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PMID: 8080094 Published · ppublish English Comparative Study Journal Article

The use of divalent cations and pH for the determination of specific yeast chitin synthetases.

Analytical biochemistry ·Vol. 219 ·No. 2 ·1994-06-00 ·Pages 368-72

Choi WJ, Cabib E

Abstract

Saccharomyces cerevisiae contains three chitin synthetases, Chs1, Chs2, and Chs3, performing different physiological functions but catalyzing the same reaction. It has been found that Ni2+ is a powerful inhibitor of Chs1 and Chs2 activity but has very little effect on the activity of Chs3, especially in the presence of Co2+. These results, together with the previous knowledge that Co2+ stimulates Chs2 and Chs3 but inhibits Chs1 and that the three synthetases differ in their pH optimum, have enabled us to formulate conditions for the specific determination of each synthetase in the presence of the others.

MeSH Terms
Cations, Divalent Chitin Synthase/analysis,metabolism Cobalt/pharmacology Enzyme Activation Hydrogen-Ion Concentration Isoenzymes/analysis,metabolism Kinetics Magnesium/pharmacology Nickel/pharmacology Saccharomyces cerevisiae/enzymology Sensitivity and Specificity Substrate Specificity Trypsin/pharmacology Uridine Diphosphate N-Acetylglucosamine/metabolism
Chemicals
Cations, Divalent Isoenzymes Cobalt Uridine Diphosphate N-Acetylglucosamine Nickel Chitin Synthase Trypsin Magnesium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Choi W J
Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.
Cabib E
Article Info
Journal
Analytical biochemistry
Abbr.
Anal Biochem
ISSN
0003-2697
Published
1994-06-00
Pages
368-72
Language
English
Region
United States
NLM ID
0370535
Subset
IM
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