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Biomedical subjects

H M Farrell

Publications and source records attributed to H M Farrell.

86 records · Page 5Linked to original sources
PubMed1977

Phosphorylation of casein by the lactating mammary gland: a review.

The lactating mammary gland synthesizes and secretes large amounts of phosphoproteins that mainly are associated with the casein fraction of milk. The free amino acids and inorganic phosphate of blood serve as building materials for casein, and the final product appears in milk as a colloidal-sized particle, the casein micelle. According to our present concept, the biosynthesis of casein occurs in two steps: synthesis of the polypeptide chain, followed by phosphate addition. Phosphate groups are transferred to the nascent casein by a protein kinase localized in the Golgi apparatus. The enzyme uses adenosine 5'-triphosphate as the phosphate donor and requires divalent cations. Neighboring amino acids may be important in determining which serine residues in casein are phosphorylated. This review discusses historical and current research on the phosphorylation of casein.

Animals↗
PubMed1976

Identification of the milk fat globule membrane proteins. I. Isolation and partial characterization of glycoprotein B.

The salt soluble proteins from the fat globule membrane of cow's milk were resolved into three fractions by Sephadex column chromatography in sodium dodecyl sulfate. One of the fractions, termed glycoprotein B, was purified by rechromatography to essentially one band on sodium dodecyl sulfate gel electrophoresis. It was found to contain 14% carbohydrate including sialic acid, mannose, galactose, glucose, glucosamine and galactosamine. The amino acid composition of glycoprotein B was determined; it has amino terminal serine and carboxyl terminal leucine. The molecular weight of this glycoprotein as estimated by sodium dodecyl sulfate gel electrophoresis is 49 500.

Amino Acids↗
PubMed1976

Removal of phosphate groups from casein with potato acid phosphatase.

Potato acid phosphatase (EC 3.1.3.2) was used to remove the eight phosphate groups from alphas1-casein. Unlike most acid phosphatases, which are active at pH 6.0 or below, potato acid phosphatase can catalyze the dephosphorylation of alphas1-casein at pH 7.0. Although phosphate inhibition is considerable (K1=0.42 mM phosphate), the phosphate ions produced by the dephosphorylation of casein can be removed by dialysis, allowing the reaction to go to completion. The dephosphorylated alphas1-casein is homogeneous on gel electrophoresis with a slower mobility than native alphas1-casein and has an amino acid composition which is identical to native alphas1-casein. Thus the removal of phosphate groups from casein does not alter its primary structure. Potato acid phosphatase also removed the phosphate groups from other phosphoproteins, such as beta-casein, riboflavin binding protein, pepsinogen, ovalbumin, and phosvitin.

Acid Phosphatase↗
PubMed1976

Composition of the milks of dairy cattle. II. Ash, calcium, magnesium, and phosphorus.

Milks from commercial dairy herds in Southeastern Pennsylvania were analyzed for ash, calcium, magnesium, and phosphorus. Milk samples were from single milkings of 151 healthy purebred cows in midlactation. The data represent market milk composition. Average values for all animals were ash .78%, calcium 1.25 g/liter, magnesium .11 g/liter, and phosphorus 1.14 g/liter. The data also were grouped and analyzed by breed and beta-lactoglobulin phenotype. Breeds differed in all inorganic components with 18 to 33 cows per breed. No differences in ash, calcium, magnesium, or phosphorus were significant when the data were grouped by beta-lactoglobulin phenotype.

Animals↗
PubMed1976

Nomemclature of the proteins of cow's milk: fourth revision.

This report reviews the nomenclature of the milk proteins of cow's milk in light of more recent advances in our knowledge. With the establishment of the primary structures of a number of these proteins, we now have a definite identification of alphas1-, kappa-, beta-, and the gamma-caseins as well as beta-lactoglobulin and alpha-lactalbumin. On the basis of new information on their primary structures and relationship to beta-casein polymorphs, changes in nomenclature have been recommended for proteins of the gamma-casein fraction. Although the primary structure serves as the unambiguous definition of proteins for which it is known, a more practical identification is necessary. We recommend that their behavior in gel electrophoresis under suitable conditions be employed for this purpose for all of the "major" milk proteins of raw skim milk except the immunoglobulins where, because of their heterogeneity and molecular genetics, physical parameters are less useful and their identification must be based upon antigenic determinants and their homology with their human counterparts. More work is needed and, with the accumulation of more information, additional changes in nomenclature can be expected for such proteins as the minor components of alphas- and kappa-caseins, alpha-lactalbumin, and the proteose-peptone fraction as well as further confirmation of the presence of immunoglobulins IgE and additional IgG subclasses. Additional components and genetic variants also can be expected.

Animals↗
PubMed1975

Composition of milks of dairy cattle. I. Protein, lactose, and fat contents and distribution of protein fraction.

Milks from commercial dairy herds in Southeastern Pennsylvania were analyzed for total protein, casein, whey protein, beta-lactoglobulin, nonprotein nitrogen, and lactose contents. Data for fat contents and milk yields were from Dairy Herd Improvement Association records for the same lactation. Milk samples were from a single milking of healthy cows (151) in midlactation. Since the remainder of the milk was returned to the bulk milk of the farm, the data represent market milk composition. The data were grouped and analyzed by breed and beta-lactoglobulin phenotype; there were 18 to 33 cows per breed. In true protein percentage, the breeds ranked: Jersey 4.07 plus or minus .49, Brown Swiss 3.84 plus or minus .47, Guernsey 3.56 plus or minus .53, Ayrshire 3.30 plus or minus .52, Milking Shorthorn 3.17 plus or minus .47, Holstein 3.07 plus or minus .43. Breeds differed in all other components and in milk yield. Brown Swiss ranked highest in yield of protein. Only whey protein and beta-lactoglobulin contents were influenced by the beta-lactoglobulin genotype with beta-lactoglobulin A greater than AB greater than B in whey protein content.

Animals↗