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1.
Meat Sci ; 149: 156-162, 2019 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-30528720

RESUMO

The objective was to examine shelf stability, cooked product yield, and sensory characteristics of beef patties that had no binder (Control), incorporated soy flour (Textured Vegetable Protein; TVP) or one of three dry potato extracts: X-TRATOS™ (potato extract), X-TRATOS™ O (potato extract with mustard), or X-TRATOS™ W (potato extract with sodium acid pyrophosphate). In retail display patties, all binders decreased discoloration and lipid oxidation compared to Control, and X-TRATOS™ O was superior (P < 0.05) to all other treatments. Cooking yield was higher (P < 0.05) in patties containing potato extracts compared with patties containing TVP, which had higher yield than Control patties. Beef patties with potato extracts were juicier (P < 0.05) than Control and TVP patties and had higher (P < 0.05) overall acceptability than Control patties. We conclude that potato extracts are effective binders for use in fresh or precooked beef patties because they improve retail shelf life, cooked product yield, and sensory characteristics.


Assuntos
Produtos da Carne/análise , Extratos Vegetais/química , Solanum tuberosum , Animais , Bovinos , Cor , Comportamento do Consumidor , Culinária , Difosfatos/química , Armazenamento de Alimentos , Humanos , Peroxidação de Lipídeos , Mostardeira , Glycine max , Água/química
2.
Meat Sci ; 135: 36-41, 2018 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-28889033

RESUMO

Our objectives were to determine the effect of post rigor calcium chloride injection or freezing on 1) sarcoplasmic calcium concentration and calpain-2 activity of beef longissimus lumborum (LL) and semimembranosus (SM) steaks aged 1, 4, and 14days post-treatment and on 2) Warner-Bratzler shear force, water holding capacity, and consumer acceptability of LL and SM steaks aged 4 and 14days post-treatment. Free calcium levels in the calcium, frozen, and control steaks averaged 1256, 127, and 121µM for the LL and 1520, 120, and 111µM for the SM, respectively. Measurable LL native calpain-2 activity was lower in calcium and frozen steaks than control steaks (P<0.01), while SM native calpain-2 activity was lowest in calcium steaks and intermediate in frozen steaks (P<0.01). LL calcium steaks were more tender (P=0.04) than control steaks. In conclusion, calcium chloride injection and freezing activate calpain-2 earlier postmortem in both muscles and calcium injection improves LL tenderness.


Assuntos
Calpaína/metabolismo , Carne Vermelha/análise , Adolescente , Adulto , Animais , Cálcio/análise , Cloreto de Cálcio/química , Calpaína/normas , Bovinos , Feminino , Congelamento , Humanos , Masculino , Pessoa de Meia-Idade , Músculo Esquelético/enzimologia , Mudanças Depois da Morte , Paladar
3.
Meat Sci ; 131: 142-145, 2017 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-28527364

RESUMO

Our objectives were to (Exp. 1) determine the effect of postmortem aging (2, 3, 4, 14, 28, and 42days) on calpain-1 and -2 activity in beef longissimus lumborum (LL) and semimembranosus (SM) steaks and (Exp. 2) determine the effect of postmortem aging for two extended periods (63 and 84days) on calpain-2 activity of beef SM steaks. Calpain-1 was not active in either muscle following 14days of aging. Native calpain-2 activity decreased (P<0.001) with longer aging periods for both the LL and SM in Exp. 1 and for the SM in Exp. 2. Autolyzed calpain-2 activity increased (P<0.001) with longer aging for the LL and SM in Exp. 1 and for the SM in Exp. 2. Our results indicate that both calpain-1 and calpain-2 may contribute to the postmortem improvement of beef tenderness, with calpain-1 being responsible for the tenderness improvement early postmortem and calpain-2 responsible for additional tenderization during extended aging.


Assuntos
Calpaína/química , Músculo Esquelético/enzimologia , Carne Vermelha/análise , Animais , Bovinos , Manipulação de Alimentos , Mudanças Depois da Morte , Fatores de Tempo
4.
Meat Sci ; 119: 110-7, 2016 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-27155799

RESUMO

The objective was to determine the influence of post-fabrication aging (2, 14, 21, 42, and 63days) on beef quality characteristics and consumer sensory perception of biceps femoris (BF) and semimembranosus (SM) steaks. Lipid oxidation and aerobic plate counts increased (P<0.05) with longer aging periods and retail display times. An aging period by day of retail display interaction (P<0.05) was observed for a* and b* values of the BF and SM. Warner-Bratzler shear force values decreased (P<0.05) with longer aging for the SM, while no difference was observed for the BF. Consumer panel results revealed that longer aging periods increased (P<0.05) acceptability of the SM, tenderness of both muscles, and tended to increase (P=0.07) juiciness of the SM. Our results show that extended aging reduces retail color stability yet has positive effects on consumer perception of tenderness of both muscles and overall acceptability of the SM.


Assuntos
Manipulação de Alimentos , Qualidade dos Alimentos , Carne Vermelha , Paladar , Adolescente , Adulto , Animais , Bovinos , Cor , Comportamento do Consumidor , Culinária , Feminino , Humanos , Concentração de Íons de Hidrogênio , Masculino , Pessoa de Meia-Idade , Músculo Esquelético , Fatores de Tempo , Adulto Jovem
5.
Meat Sci ; 107: 64-74, 2015 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-25965965

RESUMO

We hypothesized that variable composition in finishing rations, more specifically; the proportion of potato-by-product (PBP) and rumen protected histidine (His) supplementation may influence growth and meat quality attributes. Two different diets were fed (1) finishing ration with corn and barley as grains (CB, n = 20) and (2) substitution of 10% corn, DM basis, with PBP (PBP, n = 20). Additionally, half of each dietary treatment received 50 g/hd/d rumen protected His (HS, n= 20) while the other half received no supplement (NS, n = 20). Inclusion of 10% PBP or HS did not affect growth or carcass traits. Color stability was analyzed using Hunter color values as well as AMSA visual appraisal in both longissimus thoracis (LT) and gluteus medius (GM) muscles. The LT, but not the GM, of CB steers was more color stable over a 9 d simulated retail display compared to those fed a PB diet. Steers receiving HS produced significantly (P < 0.05) more color stable LT and GM steaks.


Assuntos
Cor , Suplementos Nutricionais , Histidina , Músculo Esquelético , Carne Vermelha/análise , Rúmen/metabolismo , Solanum tuberosum , Fenômenos Fisiológicos da Nutrição Animal , Animais , Bovinos , Dieta , Hordeum , Humanos , Tubérculos , Carne Vermelha/normas , Aumento de Peso , Zea mays
6.
Meat Sci ; 110: 32-9, 2015 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-26172241

RESUMO

The objective was to determine the influence of post-fabrication aging (2, 14, 21, 42, and 63 days) on beef quality characteristics and consumer sensory perception of gluteus medius (GM) and longissimus lumborum (LL) steaks. Lipid oxidation and aerobic plate counts increased (P<0.05) with longer aging periods and retail display times. An aging period by day of retail display interaction (P<0.05) was observed for a* and b* values for both muscles and L* values for the LL. Warner-Bratzler shear force values decreased (P<0.05) with longer aging for the LL, while no difference was observed for the GM. Consumer panel results demonstrated that longer aging periods increased (P<0.05) tenderness of both muscles. Our results indicate that extended aging reduces retail color stability yet has positive effects on consumer perception of tenderness of beef loin muscles.


Assuntos
Cor , Comportamento do Consumidor , Manipulação de Alimentos/métodos , Carne Vermelha/análise , Estresse Mecânico , Adolescente , Adulto , Animais , Bovinos , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Músculo Esquelético , Paladar , Fatores de Tempo , Adulto Jovem
7.
Endocrinology ; 137(4): 1385-94, 1996 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-8625915

RESUMO

Accumulation of DNA is essential for muscle growth, yet mechanisms of androgen-induced DNA accretion in skeletal muscle are unclear. The purpose of this study was to determine whether androgen receptors (AR) are present in cultured skeletal muscle satellite cells and myotubes and examine the effects of testosterone on satellite cell proliferation and differentiation. Immunoblot analysis using polyclonal AR antibodies (PG-21) revealed an immunoreactive AR protein of approximately 107 kDa in porcine satellite cells and myotubes. Immunocytochemical AR staining was confined to the nuclei of satellite cells, myotubes, and muscle-derived fibroblasts. Administration of 10(-7) M testosterone to satellite cells, myotubes, and muscle-derived fibroblasts increased immunoreactive AR. In satellite cells and myotubes, AR increased incrementally after 6, 12, and 24 h of exposure to testosterone. Testosterone (10(-10) - 10(-6) M), alone or in combination with insulin-like growth factor I, basic fibroblast growth factor, or platelet-derived growth factor-BB, had no effect (P > 0.01) on porcine satellite cell proliferation, and testosterone pretreatment for 24 h did not alter the subsequent responsiveness of cells to these growth factors. Satellite cell differentiation was depressed (20-30%) on days 2-4 of treatment with 10(-7) M testosterone. This effect was not reversible within 48 h after treatment withdrawal and replacement with control medium. These data indicate that satellite cells are direct targets for androgen action, and testosterone administration increases immunoreactive AR protein and reduces differentiation of porcine satellite cells in vitro.


Assuntos
Músculo Esquelético/citologia , Receptores Androgênicos/fisiologia , Testosterona/farmacologia , Regulação para Cima/efeitos dos fármacos , Animais , Diferenciação Celular/efeitos dos fármacos , Divisão Celular/efeitos dos fármacos , Imuno-Histoquímica , Músculo Esquelético/metabolismo , Suínos , Distribuição Tecidual
8.
Tissue Cell ; 24(2): 253-62, 1992.
Artigo em Inglês | MEDLINE | ID: mdl-1589873

RESUMO

Myogenic satellite cells were isolated from semimembranosus muscles of 4-8 week-old pigs. Muscles were ground and incubated in 0.8 mg/ml Pronase solution for 40 min at 37 degrees C. Following enzymatic digestion, cells were separated from muscle debris by differential centrifugation and sequential filtering through 500 and 53 microns nylon mesh. Primary cultures grown in 16 mm diameter cell culture wells were used to evaluate five sera, media, and substrata for their ability to promote satellite cell proliferation and differentiation. Porcine satellite cell proliferation and myotube formation were optimized in cultures grown on gelatin-coated substratum in the presence of Minimum Essential Medium-alpha supplemented with 10% fetal bovine serum (FBS) (P less than 0.01). Maximum fusion was induced by 48 hr exposure to 2% FBS, horse serum, or lamb serum. These data 1) document the first evidence that myogenic satellite cells can be isolated from porcine skeletal muscle, and 2) identify culture conditions which optimize proliferation and myotube formation of porcine satellite cells.


Assuntos
Músculos/citologia , Animais , Diferenciação Celular , Divisão Celular , Células Cultivadas , Meios de Cultura , Suínos
9.
Tissue Cell ; 20(6): 899-908, 1988.
Artigo em Inglês | MEDLINE | ID: mdl-3245037

RESUMO

Myogenic satellite cells were isolated from the pectoralis major muscle of young growing tom turkeys. These cells were capable of proliferating and forming large multinucleated myotubes in vitro. Of 36 media-sera combinations evaluated, McCoy's 5A medium containing 15% chicken serum (CS) promoted the greatest level of proliferation and subsequent myotube formation when cells were induced to differentiate (P less than 0.05). Myotube formation was maximized following exposure of cultures to Dulbecco's Modified Eagle's Medium (DMEM) containing 1% horse serum (HS; DMEM-1% HS) for 4 days. Satellite cells grown under these conditions generally resulted in cultures containing greater than 90% fused nuclei. Cells plated in the presence of DMEM-10% HS resulted in greater attachment and larger cultures (and consequently a greater fused nuclei number) when transferred to growth media than similarly grown cultures plated in McCoy's 5A medium-10% CS, regardless of substrata tested (P less than 0.05). The greatest proliferation and myotube formation was seen in cultures grown in gelatin-coated wells. Proliferation was maximized in McCoy's 5A medium containing 18% CS, although this was not significantly different than the proliferation with media containing 15% CS (P greater than 0.05). Our results (1) document that the postnatal myogenic satellite cell can be isolated from the turkey in sufficient quantities for biological studies and (2) identify culture conditions which optimize proliferation and differentiation of these cells in vitro.


Assuntos
Músculos Peitorais/citologia , Perus/anatomia & histologia , Animais , Diferenciação Celular , Divisão Celular , Células Cultivadas , Meios de Cultura , Masculino
10.
Domest Anim Endocrinol ; 7(3): 413-24, 1990 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-2167814

RESUMO

Satellite cells, isolated from the superficial pectoralis muscle of growing Nicholas tom turkeys, were cloned to obtain a pure population of myogenic cells. These cells proliferated rapidly and differentiated (fused) into myotubes typically containing 92-98% fused nuclei. Competitive binding assays were performed on near-confluent satellite cell or myotube cultures in 35 mm diameter wells by adding [125I]IGF-I along with increasing concentrations of unlabeled IGF-I, IGF-II, or insulin. Following incubation, the cultures were washed to remove the unbound hormones, solubilized with 0.5 N NaOH, and the radioactivity specifically bound was determined. Total and fused nuclei number as well as total protein were determined in parallel cultures. Our results indicate that turkey satellite cell and myotube cultures possess specific binding sites for IGF-I. Displacement of [125I]IGF-I was in the order of IGF-I greater than IGF-II greater than or equal to insulin. Although the [125I]IGF-I association constants were similar for turkey satellite cells and myotubes, a 2.8-fold decrease in the number of receptors per nuclei was observed as satellite cells differentiated into myotubes. The 50% inhibition constants for IGF-I, IGF-II, and insulin were 3.7 X 10(-9) M, 7.5 X 10(-8) M, and 8.7 X 10(-8) M for satellite cells and 3.1 X 10(-9) M, 7.5 X 10(-8) M, and 9.6 X 10(-8) M for myotubes, respectively. Receptor cross-linking analysis using disuccinimidyl suberate was performed on near-confluent satellite cell cultures incubated with [125I]IGF-I in the presence or absence of 1 X 10(-7) M IGF-I, IGF-II, or insulin. Receptor subunit species of Mr 130 kDa and 98 kDa were observed under reducing conditions (100 mM dithiothreitol) and at a Mr greater than 300 kDa (native receptor tetramer) under non-reduced conditions. Autoradiographic bands were displaced with IGF-I but not with equimolar levels of IGF-II or insulin. The results suggest that turkey satellite cells possess a type I IGF receptor.


Assuntos
Fator de Crescimento Insulin-Like I/metabolismo , Desenvolvimento Muscular , Receptores de Superfície Celular/metabolismo , Somatomedinas/metabolismo , Perus/crescimento & desenvolvimento , Animais , Autorradiografia , Ligação Competitiva , Células Cultivadas , Células Clonais , Masculino , Músculos/citologia , Receptores de Somatomedina
11.
Domest Anim Endocrinol ; 13(2): 107-26, 1996 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-8665800

RESUMO

Satellite cells are the postnatal myogenic cells, as they provide myonuclei to support skeletal muscle hypertrophy and are principal cells responsible for myofiber repair and regeneration. Even though research with satellite cells from meat animals is new, considerable data exist to suggest that these cells are regulated through both intrinsic and extrinsic mechanisms. This review covers the present status of the extrinsic factors known or postulated to modulate meat animal satellite cell growth and development.


Assuntos
Animais Domésticos , Músculo Esquelético/citologia , Animais , Matriz Extracelular/fisiologia , Substâncias de Crescimento/farmacologia , Hormônios/farmacologia , Desenvolvimento Muscular , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/crescimento & desenvolvimento , Músculo Esquelético/inervação
12.
J Anim Sci ; 77(6): 1467-73, 1999 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-10375223

RESUMO

A negative correlation exists between calpastatin activity and meat tenderness. Therefore, it is important to determine the mechanism of calpastatin inactivation in postmortem skeletal muscle. Western immunoblot analysis was performed to determine the protease(s) responsible for degradation of muscle calpastatin during postmortem storage. To accomplish this, purified calpastatin was digested with different proteases in vitro, and their pattern of calpastatin degradation was compared with that of calpastatin degradation in postmortem muscle. Polyclonal antibodies raised in mice against recombinant bovine skeletal muscle calpastatin were used to monitor calpastatin degradation. Lamb longissimus was stored at 4 degrees C and sampled at 0, 6, 12, 24, 72, 168, and 336 h postmortem. Postmortem storage produced a discrete pattern of calpastatin degradation products that included immunoreactive bands at approximately 100, 80, 65, 54, 32, and 29 kDa. Undegraded calpastatin (130 kDa) was barely detectable after 72 h of postmortem storage at 4 degrees C, and no immunoreactive calpastatin was observed by 336 h postmortem. For in vitro proteolysis, lamb longissimus calpastatin (0 h postmortem) was purified using Affi-Gel Blue chromatography. Calpastatin was digested with m-calpain, mu-calpain, cathepsin B, proteasome, trypsin, or chymotrypsin. Each of these enzymes degraded calpastatin. Immunoreactive fragments resulting from digestion of calpastatin with m- and mu-calpain were similar to each other and closely resembled those observed during postmortem aging of lamb longissimus at 4 degrees C. Digestion of calpastatin with mu-calpain reduced calpastatin activity. Degradation of calpastatin by other proteases resulted in unique patterns of immunoreactive fragments, distinct from that observed in longissimus. Thus, m- and(or) mu-calpain seem to be responsible for calpastatin degradation during postmortem storage of meat.


Assuntos
Proteínas de Ligação ao Cálcio/metabolismo , Calpaína/metabolismo , Bovinos/metabolismo , Inibidores de Cisteína Proteinase/metabolismo , Músculos/enzimologia , Animais , Western Blotting/veterinária , Calpaína/antagonistas & inibidores , Eletroforese em Gel de Poliacrilamida/veterinária , Carne/normas , Camundongos , Peso Molecular , Mudanças Depois da Morte
13.
J Anim Sci ; 74(12): 2935-42, 1996 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-8994907

RESUMO

The objective of this experiment was to test the hypothesis that meat toughening during the first 24 h postmortem results from sarcomere shortening during rigor mortis development. Eleven market-weight lambs were used to measure changes in shear force of clamped longissimus during rigor development. Within 15 min of exsanguination, while attached at both ends, each longissimus was separated from the vertebrae body and clamped between three sets of metal plates to prevent muscle shortening (six clamped sections per lamb). Five of the clamped sections were placed at -1.1 degrees C for 0, 3, 6, 12, or 24 h. After storage at their respective times at -1.1 degrees C, the samples were placed at -30 degrees C for 90 min and then at -5 degrees C for 8 d. The sixth section (168-h section) was stored at -1.1 degrees C for the first 24 h, at 4 degrees C for 144 h, and then treated the same as other sampling times. Sections were sampled for pH, sarcomere length, shear force, and Western blot analyses before and after storage at -5 degrees C. Shear force values were the same (P > .05) from 0 to 24 h (4.5 kg at 0 h to 4.9 kg at 24 h) then declined (P < .05) to 3.3 kg at 168 h postmortem. As evident by lack of statistical difference in the sarcomere lengths, we were successful in holding the muscle length constant. Western blot analyses of nebulin, vinculin, and troponin-T indicated that minimum degradation occurred through 12 h, was slightly increased by 24 h, and was relatively extensive by 168 h postmortem. Although limited proteolysis occurred during storage at -5 degrees C for 8 d, this by itself had no effect on shear force. Results indicate that shear force values do not increase during rigor development when muscle is prevented from shortening; thus, the toughening that occurs during the first 24 h of slaughter is most likely due to sarcomere shortening.


Assuntos
Tecnologia de Alimentos/métodos , Carne/normas , Músculo Esquelético/fisiologia , Rigor Mortis/veterinária , Doenças dos Ovinos/prevenção & controle , Ovinos/fisiologia , Animais , Western Blotting/métodos , Western Blotting/veterinária , Concentração de Íons de Hidrogênio , Masculino , Proteínas Musculares/análise , Músculo Esquelético/química , Músculo Esquelético/patologia , Mudanças Depois da Morte , Rigor Mortis/fisiopatologia , Rigor Mortis/prevenção & controle , Sarcômeros/ultraestrutura , Ovinos/anatomia & histologia , Doenças dos Ovinos/patologia , Doenças dos Ovinos/fisiopatologia , Temperatura , Fatores de Tempo , Troponina/análise , Troponina T , Vinculina/análise
14.
J Anim Sci ; 73(12): 3596-607, 1995 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-8655433

RESUMO

The present experiment was conducted to determine the effect of the callipyge phenotype on traits affecting muscle growth and meat tenderness. Dorset wethers (N = 40) that were either carriers or non-carriers were fed grain and slaughtered at 169 d of age. Callipyge phenotype did not affect (P > .05) slaughter weight, hot carcass weight, or weights of the heart, spleen, viscera, kidney-pelvic fat, head, and pelt; however, callipyge lambs had a higher dressing percentage and lighter lungs, liver, and kidneys (P < .01). Callipyge lambs had reduced fat thickness and marbling score and higher leg scores and longissimus area (34%). Adductor (30%), biceps femoris (42%), gluteus group (31%), longissimus (32%), psoas group (20%), quadriceps femoris (18%), semimembranosus (38%), and semitendinosus (26%) weights were higher in the callipyge phenotype (P < .01); however, phenotype did not affect (P > .05) weights of infraspinatus or supraspinatus. Longissimus pH and temperature declines were not affected (P > .05) by phenotype. Longissimus myofibril fragmentation index was lower at 1 (27%), 7 (35%), and 21 (37%) d postmortem and Warner-Bratzler shear force was higher at 1, 7, and 21 d postmortem in the callipyge phenotype (P < .01). Shear force values of callipyge lambs at 21 d postmortem tended to be greater (P = .12) than shear force values of non-carriers at 1 d postmortem . Activities of calpastatin (83%) and m-calpain (45%) were higher in the callipyge (P < .01); however mu-calpain activity was not affected (P > .05). Longissimus and semitendinosus RNA concentration, DNA content, RNA content, protein content, and the RNA:DNA ratio were higher (P < .05), but DNA concentration, protein concentration, and protein:DNA were not affected in the callipyge phenotype. The higher calpastatin activity associated with callipyge suggests that protein degradation may be reduced in the live animal. Additionally, the increased muscle DNA content associated with the callipyge phenotype suggests an increase in satellite cell proliferation, and results in an increased capacity of skeletal muscle to accumulate and maintain myofibrillar protein. These results suggests that both reduced rate of protein degradation and higher capacity for protein synthesis are consequences of the callipyge condition.


Assuntos
Carne/normas , Desenvolvimento Muscular , Músculo Esquelético/crescimento & desenvolvimento , Músculo Esquelético/patologia , Doenças dos Ovinos/patologia , Actinina/análise , Animais , Western Blotting , Peso Corporal/fisiologia , Proteínas de Ligação ao Cálcio/análise , Calpaína/análise , Conectina , Desmina/análise , Concentração de Íons de Hidrogênio , Hipertrofia/patologia , Hipertrofia/fisiopatologia , Hipertrofia/veterinária , Masculino , Fibras Musculares Esqueléticas/ultraestrutura , Proteínas Musculares/análise , Músculo Esquelético/química , Ácidos Nucleicos/análise , Fenótipo , Proteínas Quinases/análise , Ovinos , Doenças dos Ovinos/fisiopatologia , Temperatura , Troponina/análise
15.
J Anim Sci ; 81(10): 2395-400, 2003 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-14552364

RESUMO

Our objective was to determine the effect of repeated use of implants on feedlot performance and carcass characteristics of Holstein cattle. Holstein steers (n = 128) weighing an average of 211 kg were blocked by weight and randomly assigned to 16 pens. At the start of the trial (d 0), pens were assigned to one of four treatments: 1) nonimplanted control (C); 2) implant on d 0, 112, and 224 (T3); 3) implant on d 112 and 224 (T2); and 4) implant on d 224 (T1). Component TE-S implants (120 mg of trenbolone acetate and 24 mg of estradiol per implant) were used for all treatments during the 291-d feeding period. Over the course of the study, T2 and T3 cattle had greater ADG and final weights than C and T1 cattle (P < 0.05). Steers were harvested at a commercial abattoir on d 291. Hot carcass weights of T3 steers were greater than those of C and T1 steers (P < 0.05). Dressing percentage, adjusted 12th-rib fat, percentage of kidney, pelvic, and heart fat, yield grade, and longissimus color were not different among treatments (P > or = 0.26). Longissimus muscle areas (LMA) of T2 and T3 carcasses were larger than LMA of C (P < 0.01). No USDA Select carcasses were produced from C cattle, whereas the percentage of Select carcasses from implanted cattle ranged from 10 to 18%. Skeletal maturity advanced (P < 0.05) progressively with each additional implant. Steaks from T3 carcasses had a higher percentage of protein than controls (P < 0.05) and were less tender than all other treatments (P < 0.05). Repeated administration of combination trenbolone acetate and estradiol implants increased ADG and resulted in heavier carcasses with larger LMA. Administration of three successive implants decreased tenderness of Holstein beef, and resulted in more advanced skeletal maturity scores.


Assuntos
Anabolizantes/farmacologia , Bovinos/crescimento & desenvolvimento , Estradiol/farmacologia , Carne/normas , Acetato de Trembolona/análogos & derivados , Acetato de Trembolona/farmacologia , Anabolizantes/administração & dosagem , Ração Animal , Animais , Composição Corporal/efeitos dos fármacos , Combinação de Medicamentos , Implantes de Medicamento , Estradiol/administração & dosagem , Masculino , Carne/classificação , Distribuição Aleatória , Fatores de Tempo , Acetato de Trembolona/administração & dosagem , Estados Unidos , United States Department of Agriculture , Aumento de Peso/efeitos dos fármacos
16.
J Anim Sci ; 79(11): 2762-9, 2001 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-11768103

RESUMO

Over 2 yr, 45 Angus-sired steer offspring of Angus and Angus crossbred females were used to determine the effects of early weaning on feedlot performance, carcass characteristics, and economic return to the cow-calf enterprise. Steers were assigned by birth date to one of two weaning treatments: 1) weaned at an average age of 100 d (early weaned) or 2) weaned at an average age of 200 d (normally weaned). Within 36 d of weaning, steers were given ad libitum access to a high-concentrate diet (90% dry, wholeshelled corn). Steers were harvested when 12th-rib fat thickness averaged 1.27 cm within treatment as estimated by ultrasound. Carcass measurements were taken 48 h postmortem and rib steak tenderness was determined at 14 d postmortem by Warner-Bratzler shear force. Early-weaned steers had greater ADG from time of early weaning to normal weaning than suckling normally weaned steers (1.27 vs. 0.86 kg/d, respectively; P < 0.001). However, early-weaned steers tended to have lower ADG for the entire finishing period than did normally weaned steers (1.33 vs. 1.39 kg/d, respectively; P = 0.08). Compared with normally weaned steers, early-weaned steers had lower daily DMI (7.40 vs. 5.95 kg/d, respectively; P < 0.001) and lower total DMI for the finishing period (1,618 vs 1,537 kg, respectively; P < 0.05). Early-weaned steers had greater gain:feed for the finishing period than normally weaned steers (0.223 vs 0.189, respectively; P < 0.001). Carcass weights were lighter for early-weaned steers than for normally weaned steers (277.9 vs. 311.2 kg, respectively; P < 0.001). There was no difference in yield grade (3.1 vs. 3.2; P < 0.10) between treatments. All carcasses graded Low-Choice or greater, and there was no difference in the percentage of carcasses grading Mid-Choice or greater (94.5 vs 83.9% for early- and normally-weaned, respectively; P > 0.10). Warner-Bratzler shear force values were similar between treatments. Early-weaned steers had a lower cost of gain than normally weaned steers ($ 0.82 vs. 0.91/kg, respectively; P < 0.001). However, due to lighter carcass weights, early-weaned steers generated less return to the cow-calf enterprise than normally weaned steers ($ 380.89 vs 480.08/steer; P < 0.001). The early weaning of steers at 100 d of age decreased total DMI, improved gain:feed, and lowered the cost of gain; however, return to the cow-calf enterprise was decreased due to lighter carcass weights.


Assuntos
Criação de Animais Domésticos/métodos , Bovinos/crescimento & desenvolvimento , Carne/normas , Desmame , Fatores Etários , Ração Animal , Criação de Animais Domésticos/economia , Animais , Composição Corporal , Ingestão de Alimentos , Metabolismo Energético/fisiologia , Masculino , Carne/economia , Distribuição Aleatória , Aumento de Peso
17.
J Anim Sci ; 74(11): 2679-86, 1996 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-8923182

RESUMO

An indirect antibody ELISA was developed for rapid and sensitive quantification of skeletal muscle calpastatin. Polyclonal antibodies were raised in rabbits against recombinant calpastatin, corresponding to domains 2, 3, and 4 of bovine skeletal muscle calpastatin. Western blot analysis revealed that these antibodies specifically recognize an immunoreactive calpastatin protein of approximately 130 kDa in prerigor skeletal muscle extracts. The intensity of the immunoreactive bands corresponds qualitatively with assayable calpastatin activity. For ELISA development, optimum dilutions of sample, primary anti-calpastatin antibody, and peroxidase-conjugated secondary antibody were determined by titration. A dilution optimum for coating of Immulon 4 (Dynatech) plates was observed when heated muscle extracts were diluted to 2 to 4 micrograms of protein/mL and incubated for 2 h at 37 degrees C. Optimum primary (30 micrograms IgG/mL) and secondary (Sigma A-6154; 1:1000 dilution) antibody incubations were for 1 h at 37 degrees C. Tetramethylbenzidine was used as substrate and A450 of the stopped reaction product was recorded in an automated plate reader. Calpastatin ELISA results were linearly related to calpastatin activity (calpain inhibitory activity) of heated longissimus muscle homogenates from prerigor lamb (r2 = .89; n = 40) and beef aged for 24 or 48 h (r2 = .90; n = 47). Intra-assay CV was < 5% (n = 8) and inter-assay CV was < 6% (n = 5). This assay offers advantages of speed, simplicity, and sensitivity over conventional methodology for calpastatin quantification.


Assuntos
Proteínas de Ligação ao Cálcio/análise , Ensaio de Imunoadsorção Enzimática/veterinária , Músculo Esquelético/química , Animais , Anticorpos/análise , Anticorpos/imunologia , Western Blotting/veterinária , Proteínas de Ligação ao Cálcio/genética , Proteínas de Ligação ao Cálcio/metabolismo , Bovinos , Eletroforese em Gel de Poliacrilamida/veterinária , Ensaio de Imunoadsorção Enzimática/métodos , Carne/normas , Desenvolvimento Muscular , Músculo Esquelético/crescimento & desenvolvimento , Músculo Esquelético/metabolismo , Coelhos , Proteínas Recombinantes/análise , Proteínas Recombinantes/genética , Proteínas Recombinantes/imunologia , Sensibilidade e Especificidade
18.
J Anim Sci ; 76(8): 2086-93, 1998 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-9734858

RESUMO

Subjecting cloned porcine myogenic satellite cells to multiple passages leads to decreased rates of cell division and myotube formation. Because IGF have been implicated in the regulation of muscle cell proliferation and differentiation, the present study was conducted to characterize secretion of IGF-I and IGF-binding proteins (IGFBP) in cultures of cloned porcine satellite cells at two stages of multiple passaging. To this end, we obtained a single porcine satellite cell clone that demonstrated relatively high capacities for cellular proliferation and differentiation into myotubes at the fifth passage but that had greatly diminished capacities for proliferation and myotube formation by the seventh passage. The predominant IGFBP secreted by this satellite cell clone was immunologically identified as IGFBP-2, and quantities of it were increased in medium from seventh-passage cultures. Quantities of IGF-I in medium were determined with a newly developed "titration" radioimmunoassay in which interference from IGFBP was minimized by adding a range of saturating quantities of IGF-II. Medium IGF-I concentrations in seventh-passage cultures were also increased relative to the fifth-passage cultures when expressed per unit of DNA. It is hypothesized that the observed increase of IGF-I in medium likely resulted from protective sequestration of IGF-I by IGFBP-2 rather than from enhanced IGF-I secretion. In summary, these data suggest that multiple passaging of cloned porcine satellite cells results in increased secretion of IGFBP-2, which is associated with depressed cell proliferation and myotube formation, perhaps because the increased IGFBP-2 sequestered IGF-I and reduced its bioactivity.


Assuntos
Proteína 2 de Ligação a Fator de Crescimento Semelhante à Insulina/análise , Músculos/citologia , Animais , Autorradiografia/veterinária , Western Blotting/veterinária , Diferenciação Celular , Divisão Celular , Células Clonais , Meios de Cultivo Condicionados , Meios de Cultura Livres de Soro , Densitometria , Proteína 2 de Ligação a Fator de Crescimento Semelhante à Insulina/química , Proteína 2 de Ligação a Fator de Crescimento Semelhante à Insulina/metabolismo , Fator de Crescimento Insulin-Like I/análise , Fator de Crescimento Insulin-Like I/metabolismo , Fator de Crescimento Insulin-Like II/metabolismo , Peso Molecular , Músculos/metabolismo , Radioimunoensaio/veterinária , Reprodutibilidade dos Testes , Suínos
19.
Meat Sci ; 63(1): 17-22, 2003 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-22061979

RESUMO

Our objective was to determine if increased glycolytic enzyme capacity accommodates rapid glycolysis, which leads to inferior pork color and water-holding capacity. Progeny from HAL-1843 free Duroc (n=16) or Pietrain (n=16) sires were harvested over a 2-week period. Coupled enzyme assays were used to quantify total capacity of pyruvate kinase (PK) and phosphofructokinase (PFK) in the sarcoplasmic fractions and crude homogenates of longissimus muscle (LM), respectively. Capacity of PK was not correlated with LM pH (20, 45, 180 min or 24 h), purge, drip loss, or CIE L* (P > 0.2). However, PFK capacity was inversely related to fluid loss (P<0.05). This finding was unexpected, but may result from PFK becoming partially denatured and inactivated by 20 min postmortem in samples that undergo a rapid pH decline. These data indicate that lighter pork color and reduced water-holding capacity are not associated with an increase in the capacity of enzymes that catalyze regulated steps of glycolysis.

20.
J Anim Sci ; 90(5): 1617-27, 2012 May.
Artigo em Inglês | MEDLINE | ID: mdl-22147475

RESUMO

A total of 42 F(1) Red Angus progeny from sires divergent in maintenance energy (ME(M)) EPD were analyzed to determine whether selecting for sire ME(M) would alter end-product meat quality. Data from animals were grouped based on the divergence of the ME(M) EPD of their sire from the Red Angus Association-reported breed average and defined as either high or low, the assumption being that high-ME(M) cattle are less efficient because their maintenance requirements represent a larger proportion of their dietary intake. Steer progeny (n = 7) from the high group produced bottom round steaks with a greater a* (redness) color value (P = 0.02) after 5 d in a simulated retail display when compared with bottom round steaks from the low group (n = 18). Bottom round steaks from the high group had a greater b* (yellowness) color value at d 1 (P = 0.03) and d 5 (P = 0.01) of retail display. Samples from the biceps femoris were taken at 12 mo (from both steers and heifers) and 15 mo (from steers only) of age for fiber type proportion analysis. At 12 mo of age, steers from the low group had more type I fibers (P = 0.02), whereas steers from the high group had more type IIb fibers (P = 0.01). Furthermore, samples from steers in the low group at 15 mo had more type I fibers (P = 0.02), and steers from the high group maintained more type IIb fibers (P = 0.02). No changes in fiber type proportions were observed between the high- and low-ME(M) EPD heifers (n = 17). Relative mRNA abundance of genes involved in the synthesis, storage, and breakdown of glycogen were analyzed as a variable important for meat quality, but no statistical differences were observed. At 12 mo age, glycogenin (glyc) was negatively correlated with the proportion of type IIa fibers (r = -0.32 and P = 0.12) as well as with the proportion of type IIb fibers (r = -0.42 and P = 0.03) in the biceps femoris of the steers. In samples taken from the biceps femoris at 15 mo age, glyc was negatively correlated with the proportion of type IIa fibers (r = -0.42 and P = 0.03) in the steers. This indicates that relative mRNA expression of glyc may serve as a marker of muscle glycogen storage capacity in steers. Thus, selection for efficient Red Angus beef cattle based on sire ME(M) EPD does not adversely affect meat quality in F(1) progeny, based on the variables assessed in this study. Furthermore, selection for progeny from low-ME(M) EPD sires may improve fresh meat quality within Red Angus beef cattle.


Assuntos
Metabolismo Energético/genética , Carne/normas , Fibras Musculares Esqueléticas/fisiologia , Animais , Cruzamento , Bovinos/genética , Bovinos/fisiologia , Metabolismo Energético/fisiologia , Regulação da Expressão Gênica/fisiologia , Variação Genética , Glicogênio , Concentração de Íons de Hidrogênio , Lactatos , Masculino , RNA/genética , RNA/metabolismo , Reação em Cadeia da Polimerase em Tempo Real
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