The preparation and characterization of two forms of bovine galactosyl transferase.

Two molecular forms of bovine galactosyl transferase have been purified by affinity chromatography. A unique form, molecular weight 51000, is obtained from bovine colostrum. A lower molecular weight form, 41000, has been obtained by tryptic digestion of the colostral enzyme, or of the three component enzymes isolated from bovine milk. Both forms are active for N-acetyllactosamine synthase and lactose synthase. The physical characteristics, amino acid composition and steady-state kinetics of the two forms are compared. Tryptic digestion converts the galactosyl transferase to a more symmetrical form, and alters the nature of the binding of UDP-galactose to the enzyme · Mn2+ complex.

[1]  D. G. Herries,et al.  Some kinetic properties of human-milk galactosyl transferase. , 1974, European journal of biochemistry.

[2]  K. Ebner,et al.  Proteolytic conversion of the molecular forms of bovine milk galactosyltransferase. , 1973, The Journal of biological chemistry.

[3]  R. Hill,et al.  Agarose derivatives of uridine diphosphate and N-acetylglucosamine for the purification of a galactosyltransferase. , 1972, The Journal of biological chemistry.

[4]  H. Mollenhauer,et al.  ISOLATION OF GERM CELL GOLGI APPARATUS FROM SEMINIFEROUS TUBULES OF RAT TESTES , 1971, The Journal of cell biology.

[5]  V. Marchesi,et al.  Human erythrocyte membrane glycoprotein: a re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis. , 1971, Biochemical and biophysical research communications.

[6]  J. Morrison,et al.  Studies on galactosyltransferase. Kinetic investigations with N-acetylglucosamine as the galactosyl group acceptor. , 1971, The Journal of biological chemistry.

[7]  K. Brew,et al.  The complete amino acid sequence of bovine α-lactalbumin. , 1970 .

[8]  S. Roseman,et al.  Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction. , 1970, The Journal of biological chemistry.

[9]  T. W. Keenan,et al.  Localization of glycosyl transferase activities in a Golgi apparatus-rich fraction isolated from rat liver. , 1969, Biochemical and biophysical research communications.

[10]  J. Woodlock,et al.  Glycoprotein staining following electrophoresis on acrylamide gels. , 1969, Analytical biochemistry.

[11]  W. Morgan,et al.  GENETIC AND BIOCHEMICAL ASPECTS OF HUMAN BLOOD-GROUP A−, B−, H−, Lea − AND Leb− SPECIFICITY , 1969 .

[12]  H. Edelhoch,et al.  Spectroscopic determination of tryptophan and tyrosine in proteins. , 1967, Biochemistry.

[13]  S. Edelstein,et al.  The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. , 1967, The Journal of biological chemistry.

[14]  D. M. Carlson,et al.  Incorporation of D-galactose into glycoproteins. , 1965, The Journal of biological chemistry.

[15]  W. Cleland.  The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. , 1963, Biochimica et biophysica acta.

[16]  D. A. Yphantis.  RAPID DETERMINATION OF MOLECULAR WEIGHTS OF PEPTIDES AND PROTEINS * , 1960 .

[17]  D. F. Waugh.  Ultracentrifugal Characterization by Direct Measurement of Activity. I. Theoretical. , 1956 .

[18]  D. A. Yphantis,et al.  Ultracentrifugal Characterization by Direct Measurement of Activity. II. Experimental. , 1956 .

[19]  F. Smith,et al.  COLORIMETRIC METHOD FOR DETER-MINATION OF SUGAR AND RELATED SUBSTANCE , 1956 .

[20]  M. Laskowski.  Crystalline trypsin inhibitor from colostrum. , 1951, Journal of Biological Chemistry.