Lactose Synthase Activity of Galactosyltransferase from Human Parotid Saliva
- 1 February 1977
- journal article
- research article
- Published by SAGE Publications in Journal of Dental Research
- Vol. 56 (2) , 181-184
- https://doi.org/10.1177/00220345770560021301
Abstract
Galactosyltransferase in human parotid saliva catalyzed the transfer of galactose from uridine 5'-diphospho (UDP)-galactose to D-glucose in the presence of exogenous a-lactalbumin. Some albumins other than α-lactalbumin did not have an effect on the appearance of lactose-synthesizing activity.This publication has 8 references indexed in Scilit:
- Some Properties of Uridine 5'-Diphosphogalactose: N-Acetylglucosamine Galactosyltransferase in Human Parotid SalivaJournal of Dental Research, 1975
- Transglycosylation by the exo-type of β-N-acetylglucosaminidase from human parotid salivaArchives of Oral Biology, 1975
- The Presence of Uridine-5'-diphospho-galactose : N-Acetylglucosamine Galactosyltransferase in Human SalivaJournal of Dental Research, 1974
- Studies on GalactosyltransferasePublished by Elsevier ,1971
- Purification and Amino Acid Analysis of Human Parotid Saliva LysozymeJournal of Dental Research, 1970
- The role of alpha-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction.Proceedings of the National Academy of Sciences, 1968
- The Isolation and Identification of the B Protein of Lactose Synthetase as α-LactalbuminJournal of Biological Chemistry, 1967
- Resolution of a Soluble Lactose Synthetase into Two Protein Components and Solubilization of Microsomal Lactose SynthetaseJournal of Biological Chemistry, 1966