RESUMEN
Diet can influence both the qualitative and quantitative traits of ruminant meat. This study evaluated the effects of castor de-oiled cake on the meat of mixed-breed male goat kids. After 165days of diet treatment, no alterations (p>0.05) were observed in the in vivo performance, anatomic components, dissection and proximate composition of the Longissimus dorsi muscle, as well as in the color and pH of the carcasses. However, diet had an effect (p<0.05) on energy metabolites, fatty acid profile, and expression of certain proteins of the Longissimus dorsi muscle. To conclude, this study showed that the establishment of castor de-oiled cake diet for a long period to goats led to alterations in meat quality, without compromising its consumption qualities.
Asunto(s)
Dieta/veterinaria , Calidad de los Alimentos , Cabras/crecimiento & desarrollo , Carne/análisis , Desarrollo de Músculos , Músculo Esquelético/crecimiento & desarrollo , Ricinus communis/química , Agricultura/economía , Alimentación Animal/análisis , Alimentación Animal/economía , Animales , Biocombustibles/economía , Ricinus communis/efectos adversos , Productos Agrícolas/efectos adversos , Productos Agrícolas/química , Dieta/efectos adversos , Dieta/economía , Proteínas en la Dieta/análisis , Proteínas en la Dieta/metabolismo , Ácidos Grasos/análisis , Ácidos Grasos/metabolismo , Humanos , Residuos Industriales/efectos adversos , Residuos Industriales/análisis , Residuos Industriales/economía , Masculino , Músculo Esquelético/metabolismo , Valor Nutritivo , Venenos/análisis , Venenos/toxicidad , Ricina/análisis , Ricina/toxicidad , Semillas/efectos adversos , Semillas/químicaRESUMEN
The present study was conducted to evaluate the effect of de-oiled castor cake on reproductive traits of crossbreed goats. Fourteen males were grouped into two lots (n = 7/group), as described: group without de-oiled castor cake (WCC) and group fed with de-oiled castor cake (CC). Goats received two diets containing a mixture of Bermudagrass hay and concentrates with the same energy (73% total digestive nutrients) and protein content (15% crude protein) during 150 days, corresponding to ages from 40 (puberty) to 60 weeks. Blood plasma concentrations of urea, albumin, lactate dehydrogenase, creatinine, alanine aminotransferase and testosterone were determined. We also evaluated scrotal circumference, sperm parameters, quantitative aspects of spermatogenesis and daily sperm production (DSP), as well as the proteome of seminal plasma and sperm membrane. Seminal fluid and sperm proteins were analyzed by 2D SDS-PAGE and mass spectrometry. After 150 days of castor cake feeding, animals had no changes in the biochemical composition of blood plasma, suggesting the absence of intoxication by ingestion of ricin. There were no alterations in dry mater intake, weight gain, testis size, peripheral concentrations of testosterone, sperm concentration, motility and morphology. Sertoli and germ cell populations in the testis and DSP were not affected either. However, there were significant variations in the expression of five seminal plasma proteins and four sperm membrane proteins. In conclusion, the replacement of soybean meal by castor cake (with ricin concentrations of 50mg/kg) did not interfere with the growth and core reproductive development of male goats. However, the diet with ricin altered the expression of certain seminal plasma and sperm membrane proteins, which play roles in sperm function and fertilization. Lower expression of these proteins may impair the ricin-fed animals to perform as high-fertility sires.
Asunto(s)
Ricina/toxicidad , Semen/efectos de los fármacos , Espermatozoides/efectos de los fármacos , Animales , Cabras , Masculino , Proteínas de la Membrana/metabolismo , Semen/metabolismo , Maduración Sexual/efectos de los fármacos , Espermatogénesis/efectos de los fármacos , Espermatozoides/metabolismo , Testículo/citología , Testículo/efectos de los fármacos , Testosterona/sangreRESUMEN
This study was conducted to characterize the major proteins of the peccary seminal plasma, based on the semen samples collected from nine adult and reproductively sound animals. Our approach included the use of two-dimensional electrophoresis followed by Coomassie blue staining and analysis of polypeptide maps with PDQuest Software (Bio-Rad). Proteins were identified by tandem mass spectrometry (LC-MS/MS). We detected 179 protein spots per gel and 98 spots were identified by mass spectrometry, corresponding to 23 different proteins. The combined intensity of those spots accounted for 56.2±6% of the intensities of all spots and 60.9% of the intensities of spots presented in every protein map. Protein spots identified as clusterin represented 19.7±8.3% of the integrated optical densities of all spots detected in the seminal plasma maps. There was a negative association (r=-0.87; P<0.05) between the intensity of a clusterin spot and the percentage of sperm with functional membrane. Spermadhesin porcine seminal plasma protein 1 and bodhesin 2 comprised 5.4±1.9 and 8.8±3.9% of the total intensity of all spots respectively. Many proteins appeared in a polymorphic pattern, such as clusterin (27 spots), epididymal secretory glutathione peroxidase (ten spots), inter-α-trypsin inhibitor (12 spots), and IgG-binding protein (ten spots), among others. In conclusion, we presently describe the major seminal plasma proteome of the peccary, which exhibits a distinct high expression of clusterin isoforms. Knowledge of wild species reproductive biology is crucial for an understanding of their survival strategies and adaptation in a changing environment.
Asunto(s)
Artiodáctilos/metabolismo , Semen/química , Proteínas de Plasma Seminal/análisis , alfa-Globulinas/análisis , Animales , Cromatografía Liquida , Clusterina/análisis , Conservación de los Recursos Naturales , Electroforesis en Gel Bidimensional , Glutatión Peroxidasa/análisis , Linfocinas/análisis , Masculino , Mapas de Interacción de Proteínas , Isoformas de Proteínas , Proteómica/métodos , Espectrometría de Masas en TándemRESUMEN
The legume lectins from the subtribe Diocleinae, often referred to as concanavalin A-like lectins, are a typical example of highly similar proteins that show distinct biological activities. The pH-dependent oligomerization that some of these lectins undergo and the relative position of amino acids within the carbohydrate-binding site are factors that have been reported to contribute to these differences in the activities of Diocleinae lectins. In the present work, we determined the amino acid sequence and the crystal structure of the lectin of Dioclea rostrata seeds (DRL), with the aim of investigating the structural bases of the different behavior displayed by this lectin in comparison to other Diocleinae lectins and determining the reason for the distinct pH-dependent dimer-tetramer equilibrium. In addition, we discovered a novel multimeric arrangement for this lectin.
Asunto(s)
Carbohidratos/química , Dioclea/química , Multimerización de Proteína , Secuencia de Aminoácidos , Cristalografía por Rayos X , Concentración de Iones de Hidrógeno , Lectinas de Plantas/química , Lectinas de Plantas/metabolismo , Unión Proteica , Conformación Proteica , Semillas/químicaRESUMEN
Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins, which are able to interfere with hemostasis. They share significant similarity in their primary structures with C-type lectins of other animals, and also present a conserved carbohydrate recognition domain (CRD). A very well studied sv C-type lectin is the heterodimeric toxin, convulxin (CVX), from the venoms of South American rattlesnakes, Crotalus durissus terrificus and C. d. cascavella. It consists of two subunits, alfa (CVXa, 13.9 kDa) and beta (CVXb, 12.6 kDa), joined by inter and intra-chain disulfide bounds, and is arranged in a tetrameric a4b4 conformation. Convulxin is able to activate platelet and induce their aggregation by acting via p62/GPVI collagen receptor. Several cDNA precursors, homolog of CVX subunits, were cloned by PCR homology screening. As determined by computational analysis, one of them, named crotacetin b subunit, was predicted as a polypeptide with a tridimensional conformation very similar to other subunits of convulxin-like snake toxins. Crotacetin was purified from C. durissus venoms by gel permeation and reverse phase high performance liquid chromatography. The heterodimeric crotacetin is expressed in the venoms of several C. durissus subspecies, but it is prevalent in the venom of C. durissus cascavella. As inferred from homology modeling, crotacetin induces platelet aggregation but noticeably exhibits antimicrobial activity against Gram-positive and Gram-negative bacteria
Asunto(s)
Animales , Crotalus , Fosfatidilcolinas/aislamiento & purificación , Homología de Secuencia de Aminoácido , Venenos de Crotálidos/clasificación , Venenos de Crotálidos/química , Alineación de SecuenciaRESUMEN
A lectin from the red marine alga Hypnea musciformis (HML) was purified by extraction with 20 mM PBS, precipitation with 70% saturated ammonium sulphate, ion-exchange DEAE-Cellulose chromatography and RP-HPLC. The 9.3 kDa polypeptide agglutinates erythrocytes from various sources and shows oligomerization tendencies under certain MALDI-TOF/MS conditions. Preliminary N-terminal sequencing and biological assays strongly suggest that the HML may belong to a new class of algae lectins.
Asunto(s)
Lectinas/química , Lectinas/aislamiento & purificación , Rhodophyta/metabolismo , Animales , Cromatografía Líquida de Alta Presión , Cromatografía por Intercambio Iónico , Dimerización , Humanos , Estructura Terciaria de Proteína , Espectrometría de Masa por Láser de Matriz Asistida de Ionización DesorciónRESUMEN
A D-glucose/D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (alpha chain), 16-18 kDa (beta fragment) and 12-13 kDa (gamma fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.
Asunto(s)
Fabaceae/química , Lectinas/aislamiento & purificación , Semillas/química , Aminoácidos/metabolismo , Animales , Cromatografía de Afinidad , Electroforesis en Gel de Poliacrilamida , Eritrocitos/metabolismo , Fabaceae/genética , Fabaceae/metabolismo , Haptenos/metabolismo , Hemaglutinación , Humanos , Lectinas/química , Lectinas/metabolismo , Lectinas de Plantas , ConejosRESUMEN
Spermadhesins are a family of secretory proteins expressed in the male genital tract of pig, horse and bull. Their function and structure have been widely studied, especially those isolated from boar. However, there are no data concerning spermadhesins isolated from buck. Buck seminal plasma was collected and subjected to ion exchange chromatography on DEAE-Sephacel column followed by chromatography in a C18 column coupled to a HPLC system. The purification of the protein was determined by SDS-PAGE and MALDI-TOF analysis exhibiting a molecular mass of 12.5 KDa and showed to be structurally homologous to spermadhesins from boar and stallion.