Lactose synthase components in milk: concentrations of alpha-lactalbumin and beta1,4-galactosyltransferase in milk of cows from several breeds at various stages of lactation.

It is believed that milk production is determined by the number and activity of mammary secretory cells. Secretory activity, as assessed by milk volume, depends on secretion of the major osmole in milk, lactose, which is produced by lactose synthase. The amount of either of the two proteins in lactose synthase may regulate milk production. The objective of this study was to determine whether the concentrations in milk of the two components of lactose synthase, alpha-lactalbumin (alpha-LA) and beta1,4-galactosyltransferase (B4GALT), were related to genetic background, stage of lactation, breed or parity of dairy cows. alpha-Lactalbumin and B4GALT concentrations were measured by ELISA and by enzyme assays, respectively, from single milk samples. Two herds with a total of 279 cows were used in the analysis. One herd contained Ayrshire, Brown Swiss, Holstein and Jersey cows; the second herd contained two groups of cows; Holsteins selected for high milk production and Holsteins with 1960s genetics. The alpha-LA concentration in milk was greater in Jerseys and Ayrshires than in Holsteins and Brown Swiss. However, no difference in alpha-LA concentration was observed in milk from high and low genetic merit cows in the Minnesota herd or among different genetic backgrounds in the Illinois herd. beta1,4-Galactosyltransferase concentrations were similar for all groups that were analyzed. alpha-Lactalbumin concentrations were positively correlated with milk protein concentration, milk fat concentration and lactose concentration. beta1,4-Galactosyltransferase concentration in milk exhibited a strong positive correlation with number of days in milk. Although the concentration of B4GALT increased as lactation progressed, the values did not show any correlation with persistency of lactation or late lactation milk production. In conclusion, this survey shows that the two components of lactose synthase are each correlated to protein concentration and individually correlated to the concentration of other milk components and stage of lactation.

[1]  W. Hurley,et al.  Effects of suckling intensity on milk yield and piglet growth from lactation-enhanced gilts. , 2006, Journal of animal science.

[2]  J. Nørgaard,et al.  Mammary cell turnover and enzyme activity in dairy cows: effects of milking frequency and diet energy density. , 2005, Journal of dairy science.

[3]  W. Hurley,et al.  Lactational performance of first-parity transgenic gilts expressing bovine alpha-lactalbumin in their milk. , 2002, Journal of animal science.

[4]  B. Ramakrishnan,et al.  Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I. , 2001, Journal of molecular biology.

[5]  M. Wheeler,et al.  Short communication: effects of increased expression of alpha-lactalbumin in transgenic mice on milk yield and pup growth. , 2001, Journal of dairy science.

[6]  C. Knight The importance of cell division in udder development and lactation , 2000 .

[7]  H. Clausen,et al.  Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. , 1999, Biochimica et biophysica acta.

[8]  Y. Iwakura,et al.  Growth retardation and early death of β‐1, 4‐galactosyltransferase knockout mice with augmented proliferation and abnormal differentiation of epithelial cells , 1997, The EMBO journal.

[9]  P. Hasty,et al.  Targeted mutation in beta1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality. , 1997, Developmental biology.

[10]  A. Schnieke,et al.  Lactation is disrupted by alpha-lactalbumin deficiency and can be restored by human alpha-lactalbumin gene replacement in mice. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[11]  R. Bremel,et al.  Prediction of milk yields from serum beta-lactoglobulin concentrations in pregnant heifers. , 1995, Journal of dairy science.

[12]  J. Vilotte,et al.  Creation and phenotypic analysis of alpha-lactalbumin-deficient mice. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[13]  G. Bleck,et al.  Correlation of the alpha-lactalbumin (+15) polymorphism to milk production and milk composition of Holsteins. , 1993, Journal of dairy science.

[14]  David J. Miller,et al.  Complementarity between sperm surface β-l,4-galactosyl-transferase and egg-coat ZP3 mediates sperm–egg binding , 1992, Nature.

[15]  G. Smithers,et al.  Seasonal Changes in the β-Lactoglobulin, α-Lactalbumin, Glycomacropeptide, and Casein Content of Whey Protein Concentrate , 1991 .

[16]  T. Mcfadden,et al.  Influence of breed and hormones on production of milk proteins by mammary explants from prepubertal heifers. , 1989, Journal of dairy science.

[17]  D. Bauman,et al.  Effect of exogenous prolactin administration on lactational performance of dairy cows. , 1987, Domestic animal endocrinology.

[18]  K. Brew,et al.  Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[19]  P. Rainard,et al.  Physiological and Pathological Factors Influencing Bovine α-Lactalbumin and β-Lactoglobulin Concentrations in Milk , 1985 .

[20]  C. Wilde,et al.  Lactose synthesis: the possibilities of regulation. , 1980, Journal of dairy science.

[21]  C. Wilde,et al.  Lactose synthesis in the rat, and the effects of litter size and malnutrition. , 1979, The Biochemical journal.

[22]  E. M. Brown,et al.  Nomenclature of the proteins of cows' milk--sixth revision. , 1965, Journal of dairy science.

[23]  C. W. Young,et al.  Responses of Yield and Conformation to Selection for Milk in a Designed Experiment with a Control Population , 1993 .

[24]  B. Shur,et al.  Complementarity between sperm surface beta-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding. , 1992, Nature.