Topic:Casein
Casein is a family of phosphoproteins predominantly found in mammalian milk, and it constitutes a significant portion of the protein content in equine milk. In horses, casein plays a vital role in the nutritional profile of mare's milk, providing essential amino acids and serving as a primary source of protein for foals. The composition and structure of casein in equine milk can influence the digestibility and absorption of nutrients. Variations in casein content can occur due to factors such as lactation stage, diet, and individual mare differences. This page compiles peer-reviewed research studies and scholarly articles that explore the composition, function, and nutritional implications of casein in equine milk, as well as its impact on foal development and health.
Isolation and characterization of beta- and gamma-caseins from horse milk. Three groups of casein components were isolated from horse milk. Group I is almost insoluble at acid and neutral pH, and is rather heterogeneous on alkaline gels with or without sodium dodecyl sulphate. Group II shows strong similarity to beta-casein from other species, as concluded from its amino acid composition and its N- and C-terminal sequences. This group consists of five electrophoretically distinguishable forms, all containing ester phosphate groups but no carbohydrate. Group III is composed of C-terminal fragments of the beta-like (group II) fraction and probably arises from the actio...
Studies on fungal flora in hair from domestic and laboratory animals suspected of dermatophytosis. I. Dematophytes. Hairsamples of domestic and laboratory animals suspected of dermatophytosis were examined for the presence of dermatophytes. A nutritionally poor base-medium developed by the author was successfully used in the isolation and identification of dermatophytes. Casein-medium supplemented with vitamins and Sabouraud-liquid medium were used in special cases. Dermatophytes were isolated in 36 of 331 samples (10.9%). The dermatophytes recovered were Microsporum canis: 13 isolates from cat. 4 from dog. 1 from horse; Trichophyton mentagrophytes var. granulare: 3 isolates from dog, 3 from horse, 2 from g...
Response to dietary nitrogen in ponies. Utilisation of nitrogen was studied in 4 crossbred ponies. A latin square design was used to study the effects of corn gluten meal, casein or urea when added to a low protein basal diet. Apparent nitrogen digestion, nitrogen retention, total plasma protein, plasma urea and plasma-free amino acids were measured. The addition of corn gluten meal, casein or urea to the basal ration increased apparent digestion of nitrogen. Casein produced a significantly greater (P less than 0.05) nitrogen retention than corn gluten meal or urea. Plasma urea nitrogen increased significantly (P less than 0.01) in ...
Amino acid composition of casein isolated from the milks of different species. Casein was isolated from the milks of the following species: cow, horse, pig, reindeer, caribou, moose, harp seal, musk-ox, polar bear, dall sheep, and fin whale. The caseins were subjected to acid hydrolysis, the resultant amino acids were converted to their n-butyl-N-trifluoroacetyl esters, and the amino acid composition of the caseins was determined by gas chromatographic analysis of these esters. Notable among the results was the close similarity, with respect to amino acid composition, of reindeer and caribou caseins. The results of the amino acid analyses of the other caseins are present...
Identification of the PR prealbumin proteins in horse serum. The Pr protein, which is one of the major equine acidic prealbumins and which consists of a large number of phenotypes, has been studied with regard to its chemical identity. Serum samples of known Pr phenotype which had been treated with varying amounts of bovine trypsin were subjected to starch gel electrophoresis at pH 4.8. When a certain amount of trypsin was used, the Pr protein was markedly affected, whereas the other acidic prealbumins retained their normal electrophoreitic pattern. Extracts from three different regions of the acidic prealbumin field were tested by the casein precipitat...
Utilization of proteins by the equine species. Protein digestion, nitrogen retention, plasma protein, plasma urea, and plasma-free amino acids were determined for ponies fed 3 different protein supplements. Substitution of casein, corn gluten meal, or corn gluten meal plus lysine for a portion of the cornstarch in a low-protein basal ration increased apparent digestion of protein. Substitution with either casein or corn gluten meal plus lysine produced a significant increase (P less than 0.05) in nitrogen retention, whereas the corn gluten meal substitution did not. Nitrogen retention, expressed as percentage of nitrogen absorbed, was incr...
Isolation of kappa-casein-like proteins from milks of various species. Kappa-Casein-like proteins were isolated from the milks of cow, goat, reindeer, horse, rat, and rabbit. When treated with rennin, all of the isolated kappa-casein components yielded para-kappa-casein-like bands on gel electrophoresis. The rate of cleavage of these components with rennin was determined by measuring material soluble in trichloroacetic acid (macropeptide). The curves were characteristic of a limited, specific attack by rennin on these proteins. The goat and reindeer kappa-caseins were nearly as bovine kappa-casein, but the cleavage of horse, rat, and rabbit kappa-casein-like comp...
Characterization of protein phosphokinase activities in horse thyroid nuclei. The distribution of protein phosphokinase (EC 2.7.1.37) activities has been established in horse thyroid nuclei. The presence of several enzyme activities has been demonstrated, two of which are clearly distinct. The first one acts on histone as substrate and is activated by cyclic AMP. Physico-chemical properties of this nuclear cyclic AMP-dependent histone kinase and of the cytosol histone kinase are different, demonstrating the absence of a contamination from the cytosol. The second enzyme acts on casein as substrate and is not stimulated by cyclic AMP POR CYCLIC GMP. The findings are consi...
Isolation and some molecular parameters of elastase-like normal proteinases from horse blood leucocytes. Cytoplasmic granules were isolated from horse blood polymorphonuclear leucocytes by the heparin method and extracted with 0.9% NaCl by repeated freezing. Soluble proteins were separated on a column of Sephadex G-75 followed by chromatography on a column of CM-Sephadex with a NaCl gradient. Gel filtration, density-gradient centrifugation, isoelectric focusing and 0.1% sodium dodecyl sulphate/polyacrylamide-gel electrophoresis at pH 7.0 and at pH 4.5 were used to determine molecular parameters of proteinases. Three enzymes hydrolysing both casein and N-benzyloxycarbonyl-L-alanine nitrophenyl est...
Substrate specificity and modifications of the active centre of elastase-like neutral proteinases from horse blood leucocytes. Two proteinases (2A and 2B) purified from the granular fraction of horse blood leucocytes degrade casein (Km values 12.8 and 6mg/ml respectively) with maximum activity at pH 7.4 and in the presence of 2m-urea. Urea-denatured haemoglobin, fibrinogen, albumin and resorcin/fuchsin-stained elastin are digested at a slower rate. The enzymes hydrolyse synthetic substrates of elastase, N-benzyloxycarbonyl-L-alanine 4-nitrophenyl ester (Km 0.114 and 0.178 mM) and N-acetyl-tri-L-alanine methyl ester (Km 5.55 and 0.98 mM), but they do not hydrolyse synthetic substrates of trypsin, chymotrypsin and throm...