A 34-KILODALTON POLYPEPTIDE IS ASSOCIATED WITH 1,3-BETA-GLUCAN SYNTHASE ACTIVITY FROM THE FUNGUS SAPROLEGNIA-MONOICA

Authors
BULONE V FEVRE M
Citation
V. Bulone et M. Fevre, A 34-KILODALTON POLYPEPTIDE IS ASSOCIATED WITH 1,3-BETA-GLUCAN SYNTHASE ACTIVITY FROM THE FUNGUS SAPROLEGNIA-MONOICA, FEMS microbiology letters, 140(2-3), 1996, pp. 145-150
Citations number
13
Categorie Soggetti
Microbiology
Journal title
FEMS microbiology letters → ACNP
ISSN journal
03781097
Volume
140
Issue
2-3
Year of publication
1996
Pages
145 - 150
Database
ISI
SICI code
0378-1097(1996)140:2-3<145:A3PIAW>2.0.ZU;2-I
Abstract
Three major polypeptides of 34, 48 and 50 kDa which appear to copurify with 1,3-beta-glucan synthase activity were isolated by glycerol grad ient centrifugation of Chaps-solubilized proteins from the fungus Sapr olegnia monoica. The antiserum produced against the 34-kDa polypeptide revealed by protein immunoblotting that this polypeptide copurified w ith 1,3-beta-glucan synthase during enzyme purification. This antiseru m adsorbs the enzymatic activity as well as the 48- and 50-kDa polypep tides. These results indicate that the 34-kDa peptide is a component o f the multisubunit protein complex involved in 1,3-beta-glucan synthas e activity.