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2.
Poult Sci ; 94(11): 2816-20, 2015 Nov.
Article in English | MEDLINE | ID: mdl-26500279

ABSTRACT

The deboning of broiler chicken wings, including drumettes and winglets, is not common in the poultry processing industry. However, consumers who like convenient foods may be interested in boneless products. Samples of broiler wings were deboned by articular cartilage dislocation and periosteum stripping without cutting skin and muscles to obtain boneless drumettes and winglets, with each having inner space formed by bone removal. The average weight of bone-in winglets (30.7 g) was less (P < 0.05) than that of bone-in drumettes (39.9 g), whereas the average percentage of boneless product was less (P < 0.05) in the drumettes (74.9) than in the winglets (80.1). There was a smaller number of muscles in the drumettes than in the winglets, but major muscles in the drumettes were larger than any muscles in the winglets. The average weight of muscle was greater (P < 0.05) and that of skin was less (P < 0.05) in the drumettes than in the winglets, and thus the muscle/skin ratio was approximately twice as high (P < 0.05) in the drumettes. The size and shape were different between the bone-in and boneless products, as expected. When a cooked product was examined, no appreciable inner space (resulting from bone removal) was seen on its transverse section. The advantages of boneless wing products over bone-in wing products were discussed. It was concluded that the method described in the present study is useful for the production of high-quality boneless wing products.


Subject(s)
Bone and Bones , Chickens , Food Handling/methods , Muscle, Skeletal , Wings, Animal , Animals , Periosteum
3.
Br Poult Sci ; 55(1): 54-8, 2014 Feb.
Article in English | MEDLINE | ID: mdl-24392803

ABSTRACT

1. The content of chondroitin sulphate (CS), known as a nutraceutical, was estimated in broiler chicken carcasses by analysing sulphated glycosaminoglycan uronic acid in posterior sternum (keel) cartilage and bones from 4 parts (wing, leg, front and hind) of carcasses. 2. The results of the present study suggested that approximately 0.63 g CS uronic acid (or 1.9 g as CS) can be extracted from a 1.66 kg whole broiler chicken carcass. The amount of extractable CS from keel cartilage, which has been reported as a valuable source of CS in broiler chicken carcasses, was surprisingly low (<10% of total CS).


Subject(s)
Bone and Bones/chemistry , Cartilage/chemistry , Chickens/metabolism , Chondroitin Sulfates/metabolism , Animals , Chromatography, Ion Exchange/veterinary , Glycosaminoglycans/analysis , Organ Specificity , Tissue Distribution , Uronic Acids/analysis
4.
Poult Sci ; 91(11): 2938-41, 2012 Nov.
Article in English | MEDLINE | ID: mdl-23091153

ABSTRACT

The yield of deboned meat is an important economic factor affecting the profit of the meat industry. This study was undertaken to determine whether the yield of boneless meat from broiler chicken leg (thigh and drumstick) and wing (drumette and winglet) is improved by introducing a new deboning method consisting of articular cartilage dislocation followed by stripping periosteum. A total of 44 broiler chicken carcasses were used in the deboning experiment. Right and left legs or wings from the first 22 carcasses were assigned to the new and ordinary hand deboning methods, respectively. For the remaining 22 carcasses, right and left legs or wings were assigned to the ordinary and new methods, respectively. The weight of residue, composed of bone and small amounts of cartilage and noncartilaginous tissues obtained after deboning, was then compared between the right and left legs or wings to see the difference between the 2 methods. The removal of tibia, fibula, humerus, radius, or ulna resulted in formation of a hollow in boneless meat obtained. There was no difference (P > 0.05) between the right and left legs or wings in the weight of residue obtained after deboning as expected. The weight of residue was less (P < 0.05) with the new method compared with the ordinary method in all chicken parts examined. The difference of residue weight between the 2 methods accounted for 10, 12, 14, and 21% of the weight of residue obtained by the ordinary method in thigh, drumstick, drumette, and winglet, respectively. The new method may be useful to deboners at home kitchens as well as the poultry meat industry. The present study also showed the development of a secondary ossification center at the proximal end of the carpometacarpus of chickens. This is, to our knowledge, the first report of development of secondary ossification center in chicken wings.


Subject(s)
Bone and Bones , Cartilage, Articular , Food Handling/methods , Meat , Periosteum , Animals , Chickens , Food Technology
5.
FEBS Lett ; 579(5): 1124-8, 2005 Feb 14.
Article in English | MEDLINE | ID: mdl-15710400

ABSTRACT

Bacterial fructosyltransferase enzymes belonging to glycoside hydrolase family 68 (GH68) are not known to require a metal cofactor. Here, we show that Ca2+ ions play an important structural role in the Lactobacillus reuteri 121 levansucrase (Lev) and inulosucrase (Inu) enzymes. Analysis of the Bacillus subtilis Lev 3D structure [Meng, G. and Futterer, K. (2003) Nat. Struct. Biol. 10, 935-941] has provided evidence for the presence of a bound metal ion, most likely Ca2+. Characterization of site-directed mutants in the putative Ca2+ ion-binding sites of Lb. reuteri Lev and Inu revealed that the Inu Asp520 and Lev Asp500 residues play an important role in Ca2+ binding. Sequence alignments of family GH68 proteins showed that this Ca2+ ion-binding site is (largely) present only in proteins of Gram-positive origin.


Subject(s)
Calcium/pharmacology , Hexosyltransferases/genetics , Hexosyltransferases/metabolism , Lactobacillus/enzymology , Mutation/genetics , Amino Acid Sequence , Binding Sites , Calcium/metabolism , Edetic Acid/pharmacology , Enzyme Stability/drug effects , Hexosyltransferases/chemistry , Hexosyltransferases/classification , Ion Transport , Lactobacillus/genetics , Molecular Sequence Data , Protein Denaturation/drug effects , Sequence Alignment , Temperature
6.
FEBS Lett ; 560(1-3): 131-3, 2004 Feb 27.
Article in English | MEDLINE | ID: mdl-14988011

ABSTRACT

Bacterial fructosyltransferases (FTFs) are retaining-type glycosidases that belong to family 68 of glycoside hydrolases. Recently, the high-resolution 3D structure of the Bacillus subtilis levansucrase has been solved [Meng, G. and Futterer, K., Nat. Struct. Biol. 10 (2003) 935-941]. Based on this structure, the catalytic nucleophile, general acid/base catalyst, and transition state stabilizer were identified. However, a detailed characterization of site-directed mutants of the catalytic nucleophile has not been presented for any FTF enzyme. We have constructed site-directed mutants of the three putative catalytic residues of the Lactobacillus reuteri 121 levansucrase and inulosucrase and characterized the mutant proteins. Changing the putative catalytic nucleophiles D272 (inulosucrase) and D249 (levansucrase) into their amido counterparts resulted in a 1.5-4x10(5) times reduction of total sucrase activity.


Subject(s)
Hexosyltransferases/chemistry , Hexosyltransferases/genetics , Lactobacillus/enzymology , Lactobacillus/genetics , Amino Acid Motifs , Amino Acid Sequence , Amino Acid Substitution , Catalysis , Circular Dichroism , Cloning, Molecular , Conserved Sequence , Escherichia coli/genetics , Gene Expression , Genes, Bacterial , Hexosyltransferases/isolation & purification , Hexosyltransferases/metabolism , Kinetics , Molecular Sequence Data , Mutagenesis, Site-Directed , Sequence Homology, Amino Acid , Substrate Specificity
7.
Poult Sci ; 82(3): 510-4, 2003 Mar.
Article in English | MEDLINE | ID: mdl-12705414

ABSTRACT

This study was undertaken to determine the occurrence of uronic acid in chicken eggshell membranes and to compare chemical compositions among the inner and outer eggshell membranes and the organic matter of eggshell. We report here for the first time the occurrence of uronic acid in chicken eggshell membranes. Uronic acid concentrations were similar (P > 0.05) between the inner shell membrane and outer shell membrane but approximately fivefold higher (P < 0.05) in the organic matter of eggshell. Sialic acid concentrations were the highest (P < 0.05) in the organic matter of eggshell and higher (P < 0.05) in the inner than in the outer shell membrane. Nitrogen concentrations were the lowest (P < 0.05) in the organic matter of eggshell but relatively constant between the two shell membranes. Amino acid analysis showed that the contents of glycine and alanine were higher (P < 0.05) and those of proline and hydroxyproline were lower (P < 0.05) in the organic matter of eggshell compared to shell membranes.


Subject(s)
Chickens , Egg Shell/chemistry , Uronic Acids/analysis , Alanine/analysis , Animals , Glycine/analysis , Hydroxyproline/analysis , Membranes/chemistry , N-Acetylneuraminic Acid/analysis , Nitrogen/analysis , Proline/analysis
8.
Poult Sci ; 81(5): 709-14, 2002 May.
Article in English | MEDLINE | ID: mdl-12033422

ABSTRACT

Galactosaminoglycans, isolated from decalcified chicken eggshell by papain digestion and ion-exchange chromatography, were fractionated by selective precipitation at varying concentrations of ethanol and characterized by chemical and enzymatic methods. The eggshell contained 0.15 microg galactosaminoglycan uronic acid/mg dry weight. Most (to approximately 87% of total) galactosaminoglycans were found to be chondroitin sulfate-dermatan sulfate copolymers with iduronic acid contents being approximately 20 to 30% of uronic acid. The remaining (to approximately 12% of total) galactosaminoglycans were chondroitin sulfate-dermatan sulfate copolymers with higher iduronic acid contents averaging 59% of uronic acid. Results of chondroitinase-ABC digestion demonstrated 4-sulfated disaccharides to be the major repeating units in the chicken eggshell galactosaminoglycans.


Subject(s)
Dermatan Sulfate/analogs & derivatives , Egg Shell/chemistry , Polysaccharides/analysis , Animals , Chemical Fractionation , Chickens , Chondroitin Sulfates/analysis , Chromatography, Ion Exchange/methods , Chromatography, Ion Exchange/veterinary , Dermatan Sulfate/analysis , Electrophoresis, Cellulose Acetate/veterinary , Ethanol/chemistry , Hyaluronic Acid/analysis , Iduronic Acid/analysis , Papain/metabolism , Uronic Acids/analysis
9.
J Neuropathol Exp Neurol ; 60(9): 906-16, 2001 Sep.
Article in English | MEDLINE | ID: mdl-11556547

ABSTRACT

The enzyme argininosuccinate synthetase (ASS) is the rate limiting enzyme in the metabolic pathway leading from L-citrulline to L-arginine, the physiological substrate of all isoforms of nitric oxide synthases (NOS). ASS and inducible NOS (iNOS) expression in neurons and glia was investigated by immunohistochemistry in brains of Alzheimer disease (AD) patients and nondemented, age-matched controls. In 3 areas examined (hippocampus, frontal, and entorhinal cortex), a marked increase in neuronal ASS and iNOS expression was observed in AD brains. GFAP-positive astrocytes expressing ASS were not increased in AD brains versus controls, whereas the number of iNOS expressing GFAP-positive astrocytes was significantly higher in AD brains. Density measurements revealed that ASS expression levels were significantly higher in glial cells of AD brains. Colocalization of ASS and iNOS immunoreactivity was detectable in neurons and glia. Occasionally, both ASS-and iNOS expression was detectable in CD 68-positive activated microglia cells in close proximity to senile plaques. These results suggest that neurons and astrocytes express ASS in human brain constitutively, whereas neuronal and glial ASS expression increases parallel to iNOS expression in AD. Because an adequate supply of L-arginine is indispensable for prolonged NO generation, coinduction of ASS enables cells to sustain NO generation during AD by replenishing necessary supply of L-arginine.


Subject(s)
Alzheimer Disease/metabolism , Argininosuccinate Synthase/metabolism , Neuroglia/enzymology , Neurons/enzymology , Nitric Oxide Synthase/metabolism , Aged , Aged, 80 and over , Alzheimer Disease/pathology , Amyloid beta-Peptides/analysis , Antigens, CD/analysis , Antigens, Differentiation, Myelomonocytic/analysis , Arginine/metabolism , Argininosuccinate Synthase/analysis , Citrulline/metabolism , Encephalitis/metabolism , Encephalitis/pathology , Entorhinal Cortex/enzymology , Entorhinal Cortex/pathology , Frontal Lobe/enzymology , Frontal Lobe/pathology , Glial Fibrillary Acidic Protein/analysis , Hippocampus/enzymology , Hippocampus/pathology , Humans , Neuroglia/chemistry , Neuroglia/pathology , Neurons/chemistry , Neurons/pathology , Nitric Oxide Synthase/analysis , Nitric Oxide Synthase Type II , Peptide Fragments/analysis
10.
J Neurosci ; 21(15): 5389-96, 2001 Aug 01.
Article in English | MEDLINE | ID: mdl-11466410

ABSTRACT

Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine disorder caused by a CAG repeat expansion in the coding region of a gene encoding ataxin-3. To study putative alterations of gene expression induced by expanded ataxin-3, we performed PCR-based cDNA subtractive hybridization in a cell culture model of SCA3. In rat mesencephalic CSM14.1 cells stably expressing expanded ataxin-3, we found a significant upregulation of mRNAs encoding the endopeptidase matrix metalloproteinase 2 (MMP-2), the transmembrane protein amyloid precursor protein, the interleukin-1 receptor-related Fos-inducible transcript, and the cytokine stromal cell-derived factor 1alpha (SDF1alpha). Immunohistochemical studies of the corresponding or associated proteins in human SCA3 brain tissue confirmed these findings, showing increased expression of MMP-2 and amyloid beta-protein (Abeta) in pontine neurons containing nuclear inclusions. In addition, extracellular Abeta-immunoreactive deposits were detected in human SCA3 pons. Furthermore, pontine neurons of SCA3 brains strongly expressed the antiinflammatory interleukin-1 receptor antagonist, the proinflammatory cytokine interleukin-1beta, and the proinflammatory chemokine SDF1. Finally, increased numbers of reactive astrocytes and activated microglial cells were found in SCA3 pons. These results suggest that inflammatory processes are involved in the pathogenesis of SCA3.


Subject(s)
Brain/metabolism , Inflammation/metabolism , Machado-Joseph Disease/metabolism , Membrane Proteins , Nerve Tissue Proteins/biosynthesis , Up-Regulation , Amyloid beta-Protein Precursor/genetics , Amyloid beta-Protein Precursor/metabolism , Animals , Ataxin-3 , Brain/pathology , Cells, Cultured , Chemokine CXCL12 , Chemokines, CXC/genetics , Chemokines, CXC/metabolism , Gene Expression Profiling , Humans , Immunohistochemistry , Inflammation/genetics , Interleukin-1 Receptor-Like 1 Protein , Interleukin-18 Receptor alpha Subunit , Machado-Joseph Disease/pathology , Matrix Metalloproteinase 2/genetics , Matrix Metalloproteinase 2/metabolism , Nerve Tissue Proteins/genetics , Neurons/metabolism , Neurons/pathology , Nuclear Proteins , Pons/metabolism , Pons/pathology , Proteins/genetics , Proteins/metabolism , RNA, Messenger/metabolism , Rats , Receptors, Cell Surface , Receptors, Interleukin , Receptors, Interleukin-18 , Repressor Proteins , Transcription Factors , Trinucleotide Repeat Expansion/genetics
11.
Poult Sci ; 80(5): 681-4, 2001 May.
Article in English | MEDLINE | ID: mdl-11372722

ABSTRACT

The objectives of this study were to analyze glycosaminoglycan (GAG) and mineral composition in the chicken eggshell. Eggshells were decalcified with acetic acid, and GAG was extracted from the decalcified shell by digestion with papain. The eggshell contained an average of 0.024% of its dry weight as uronic acid, a carbohydrate moiety of GAG. The eggshell GAG consisted of approximately 48% hyaluronic acid and and 52% galactosaminoglycan. In the latter, chondroitin sulfate-dermatan sulfate copolymers were the major galactosaminoglycans with dermatan sulfate disaccharide as a relatively minor component. The inorganic material recovered after decalcification accounted for approximately 140% of dry weight of the eggshell and contained 24.11% calcium, 0.04% phosphorous, and 0.23% magnesium, with an undetectable amount of nitrogen.


Subject(s)
Egg Shell/chemistry , Glycosaminoglycans/analysis , Minerals/analysis , Acetates/pharmacology , Animals , Chickens , Chondroitin Sulfates/analysis , Chromatography/methods , Chromatography/veterinary , Hyaluronic Acid/analysis , Uronic Acids/analysis
12.
J Agric Food Chem ; 47(7): 2613-6, 1999 Jul.
Article in English | MEDLINE | ID: mdl-10552534

ABSTRACT

Determination of sialic acid in sweet whey is useful as the concentration of sialic acid reflects the amount of glycomacropeptide (GMP) present. In this study, the concentration of total sialic acid was determined by the thiobarbituric acid reaction after dialysis of samples in water, and the concentration of GMP sialic acid was estimated by gel chromatography on Sephacryl S-200. Concentrations of total and GMP sialic acid determined in a sweet whey sample prepared from fresh milk were 2.0 and 1.5 microg/mg of dry weight, respectively. Analysis of commercial samples showed that the concentration of total sialic acid in sweet whey was 9 times lower than that in whey protein concentrate but 18 times higher than that in whey permeate. A similar trend was observed in the variation of GMP sialic acid concentration between sweet whey and why protein concentrate. The concentration of sialic acid differed 10 times between two samples of whey protein isolate.


Subject(s)
Dairy Products/analysis , N-Acetylneuraminic Acid/analysis , Thiobarbiturates/chemistry , Chromatography, Gel , Chromatography, Ion Exchange
13.
Z Ernahrungswiss ; 34(3): 224-30, 1995 Sep.
Article in English | MEDLINE | ID: mdl-7502545

ABSTRACT

Four barrows, average initial weight 35 kg, were fitted with permanent pancreatic re-entrant cannulas and used to determine the effect of level and quality of dietary fat on exocrine pancreatic secretions. The pigs were fed four corn starch-based diets that contained 15% crude protein from isolated soy protein. Diet 1 contained no canola oil (C-0); diet 2, 15% canola oil (C-15); diet 3, 15% canola oil that was heated under vacuum at 180 degrees C for 12 h (C-15/12); diet 4, 15% canola oil that was heated under vacuum at 180 degrees C for 24 h (C-15/24). Heat treatment resulted in a 4- to 5-fold increase in the content of malonaldehyde which is derived from the oxidation of fatty acids and which is closely related to odour and rancidity in lipids. The experiment was carried out according to a 4 x 4 Latin square design. The pigs were fed twice daily, at 08:00 and 20:00 h, 900 g each meal. Following an adaptation period of 7 d, pancreatic juice was collected continuously for 24 h at 2-h intervals from 08:00 on d 8 until 08:00 on d 9 and from 08:00 on d 10 until 08:00 on d 11 during each experimental period. The volume of secretion of pancreatic juice peaked 6-10 h postprandially and was similar (P > .05) during day (08:00-20:00 h) and night (20:00-08:00 h). Replacement of 15% starch by 15% canola oil resulted in a decrease (P < .05) in the secretion of alpha-amylase and an increase (P < .05) in the secretion of lipase. The inclusion of oxidized fat caused a further increase (P < .05) in total lipase activities. It can be concluded that the exocrine pancreas is able to adapt to variations in the level and quality of dietary lipids.


Subject(s)
Animal Feed , Fatty Acids, Monounsaturated/pharmacology , Malondialdehyde/pharmacology , Pancreatic Juice/drug effects , Adaptation, Physiological/drug effects , Animals , Lipase/metabolism , Male , Pancreatic Juice/metabolism , Rapeseed Oil , Secretory Rate/drug effects , Swine , alpha-Amylases/metabolism
14.
J Anim Sci ; 68(10): 3421-8, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2254212

ABSTRACT

Eight male Holstein calves (body weight 68 +/- 5 kg; age 75 +/- 6 d), each with a permanent re-entrant pancreatic cannula and T-type ileal and duodenal cannulas, were used in a crossover design with four animals per group to determine amino acid kinetics and digestibilities in the digestive tract of calves fed soybean meal (SBM) and canola meal (CM) protein. The SBM and CM diets were fed twice daily at a level of 900 g at each feeding time (air-dry basis). With the exception of methionine, crude protein and amino acid flows at the proximal duodenum, expressed as a percentage of intake, were not influenced by dietary protein source. Apparent ileal and total tract digestibilities of CP and amino acids were reduced (P less than .05) by feeding CM compared to SBM, but apparent ileal digestibility of methionine was not affected by dietary protein source. Except for methionine, net disappearance of all amino acids in the small intestine, relative to the amount fed, was higher for the SBM diet than for the CM diet. Net disappearance or synthesis of amino acids in the large intestine were not affected by dietary protein source. Similarly, dietary protein source did not affect (P greater than .05) the secretion of pancreatic juice or concentrations of protein, chymotrypsin and trypsin in pancreatic juice. Soybean meal protein has higher ileal and total gastrointestinal tract digestibility than CM protein for young, growing calves.


Subject(s)
Amino Acids/metabolism , Cattle/metabolism , Dietary Proteins/metabolism , Digestion , Digestive System/metabolism , Plant Proteins, Dietary/metabolism , Animal Feed , Animals , Male , Soybean Proteins , Glycine max
15.
J Anim Sci ; 67(6): 1634-41, 1989 Jun.
Article in English | MEDLINE | ID: mdl-2768121

ABSTRACT

The influence of replacement of milk protein by isolated soy protein on digestion and pancreatic enzyme secretion was determined in nine Holstein male calves. Calves (average weight 47 kg) were fitted with permanent re-entrant pancreatic and a T-type cannula in the distal ileum at 6 to 10 d of age. Following a 2-wk recuperation period, the calves were fed three milk replacers in a triplicated 3 x 3 latin square. Experimental diets consisted of a control, in which 100% of the CP originated from spray-dried skim milk powder (SM), and the test diets, in which 50% (SM/ISP) or 100% (ISP) of the skim milk protein was replaced by isolated soy protein. Each experimental period lasted 2 wk. Replacement of SM protein by ISP decreased (P less than .05) the digestibilities of protein and most amino acids. Ileal digestibilities of total indispensable amino acids for SM, SM/ISP and ISP diets were 82.1, 75.8 and 61.8%, respectively, and total tract digestibilities of total indispensable amino acids were 90.0, 82.6 and 74.0%, respectively. Including ISP did not affect (P greater than .05) the volume of secretion of pancreatic juice, protein or chymotrypsin; however, the secretion of trypsin decreased (P less than .05). Reduction in trypsin secretion may be responsible, in part, for the lower amino acid digestibilities in milk replacers containing isolated soy protein.


Subject(s)
Animal Feed , Cattle/metabolism , Digestion , Glycine max , Plant Proteins, Dietary/metabolism , Amino Acids/metabolism , Animals , Catheterization/veterinary , Chymotrypsin/analysis , Ileum/metabolism , Male , Milk/analysis , Milk Proteins/metabolism , Pancreatic Juice/analysis , Plant Proteins, Dietary/analysis , Soybean Proteins , Trypsin/analysis
16.
J Anim Sci ; 66(10): 2583-9, 1988 Oct.
Article in English | MEDLINE | ID: mdl-3198538

ABSTRACT

Studies were carried out with six growing barrows fitted with a simple T-cannula 5 to 10 cm anterior to the ileo-cecal sphincter. In Exp. 1, the digestibility of biotin was determined in three cornstarch-based diets formulated to contain 16% CP by supplementation with soybean meal (SBM), meat and bone meal (MBM) and canola meal (CM). In Exp. 2 the digestibility of biotin was determined in three diets that contained 96.8% barley, corn or wheat. Experiments 1 and 2 were conducted according to a replicated 3 X 3 latin square design. In Exp. 3 pigs were fed a cornstarch-based diet supplemented with 12% vitamin-free casein to determine the amount of endogenous biotin. In Exp. 4 the digestibility of supplemental biotin was determined. There was a small amount of endogenous biotin in ileal digesta, 11 micrograms/kg DMI. Digestibilities of biotin determined at the distal ileum (apparent digestibilities corrected for endogenous biotin) were 55.4, 2.7 and 3.9% in SBM, MBM and CM, respectively, and 4.8, 4.0 and 21.6% in barley, corn and wheat, respectively. The digestibility of supplemental biotin was 93.5%. There was a large increase in the level of biotin between digesta collected from the distal ileum and in feces, ranging from 138 to 324 micrograms/kg DMI. With the exception of the CM diet, this increase exceeded dietary biotin intake. Biotin in many feedstuffs was not available in the small intestine.


Subject(s)
Biotin/metabolism , Dietary Proteins/metabolism , Digestion , Edible Grain , Swine/metabolism , Animals , Male
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