Proteolytic Activation and Inactivation of Chitin Synthase from Neurospora crassa
- 1 August 1979
- journal article
- research article
- Published by Microbiology Society in Journal of General Microbiology
- Vol. 113 (2) , 339-345
- https://doi.org/10.1099/00221287-113-2-339
Abstract
The proteolytic activation and inactivation of chitin synthase from N. crassa was studied. Chitin synthase was found mostly in an inactive form which could be activated either endogenously or by the addition of exogenous proteases. The addition of protease inhibitors prevented the endogenous activation of the enzyme. The stability of the inactive enzyme improved when buffers of pH values between 8.2-9.5 were employed. The inactive enzyme was mainly associated with membranous fractions.This publication has 7 references indexed in Scilit:
- Purification and properties of an inhibitory protein of chitin synthetase from Mucor rouxiiBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Distribution and Activation of Chitin Synthase in Protoplast Fractions Released during the Lytic Digestion of Aspergillus nidulans HyphaeJournal of General Microbiology, 1978
- Chitin Synthesis in Candida albicans : Comparison of Yeast and Hyphal FormsJournal of Bacteriology, 1978
- Chitin biosynthesis in protoplasts and subcellular fractions of Aspergillus fumigatusBiochemical Journal, 1977
- Properties of chitin synthetase in isolated chitosomes from yeast cells of Mucor rouxii.Journal of Biological Chemistry, 1977
- Proteolytic Activation and Inactivation of Chitin Synthetase from Mucor rouxiiJournal of General Microbiology, 1976
- The Synthesis of Chitin by Particulate Preparations of Allomyces macrogynus*Biochemistry, 1966