Some properties of uridine 5'-diphosphogalactose: N-acetylglucosamine galactosyltransferase in human parotid saliva
- PMID: 239976
- DOI: 10.1177/00220345750540041901
Some properties of uridine 5'-diphosphogalactose: N-acetylglucosamine galactosyltransferase in human parotid saliva
Abstract
Uridine 5'-diphospho (UDP)-galactose: N-acetylglucosamine galactosyltransferase was separated from human parotid saliva and partially purified. The optimum pH of the enzyme was 7.5. The enzyme required a specific acceptor, and its activity was activated by manganese and magnesium ions.
Similar articles
-
[Purification and some properties of uridine diphosphate galactose-glycoprotein galactosyltransferase isolated from human parotid saliva].Osaka Daigaku Shigaku Zasshi. 1978 Dec;23(2):195-212. Osaka Daigaku Shigaku Zasshi. 1978. PMID: 118243 Japanese. No abstract available.
-
Lactose synthase activity of galactosyltransferase from human parotid saliva.J Dent Res. 1977 Feb;56(2):181-4. doi: 10.1177/00220345770560021301. J Dent Res. 1977. PMID: 402403
-
Characterization of UDP-galactose:2-acetamido-2-deoxy-D-glucose 3 beta-galactosyltransferase from pig trachea.J Biol Chem. 1983 Aug 25;258(16):9893-8. J Biol Chem. 1983. PMID: 6411707
-
Structure and catalytic cycle of beta-1,4-galactosyltransferase.Curr Opin Struct Biol. 2004 Oct;14(5):593-600. doi: 10.1016/j.sbi.2004.09.006. Curr Opin Struct Biol. 2004. PMID: 15465321 Review.
-
Beta-1,4-galactosyltransferase and lactose synthase: molecular mechanical devices.Biochem Biophys Res Commun. 2002 Mar 15;291(5):1113-8. doi: 10.1006/bbrc.2002.6506. Biochem Biophys Res Commun. 2002. PMID: 11883930 Review.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources