ELECTROPHORETIC CHARACTERIZATION OF ENDO-(1,4)-BETA-GLUCANASES SECRETED DURING ASSIMILATIVE GROWTH AND ANTHERIDIOL-INDUCED BRANCHING IN ACHLYA-AMBISEXUALIS

Authors
Citation
Tw. Hill, ELECTROPHORETIC CHARACTERIZATION OF ENDO-(1,4)-BETA-GLUCANASES SECRETED DURING ASSIMILATIVE GROWTH AND ANTHERIDIOL-INDUCED BRANCHING IN ACHLYA-AMBISEXUALIS, Canadian journal of microbiology, 42(6), 1996, pp. 557-561
Citations number
28
Categorie Soggetti
Microbiology,Immunology,"Biothechnology & Applied Migrobiology",Biology
ISSN journal
00084166
Volume
42
Issue
6
Year of publication
1996
Pages
557 - 561
Database
ISI
SICI code
0008-4166(1996)42:6<557:ECOES>2.0.ZU;2-H
Abstract
Secreted endo-(1,4)-beta-glucanases (''cellulases'') of Achlya ambisex ualis were analyzed by a technique that permits visualization of enzym e activity in situ after electrophoresis in gels containing sodium dod ecyl sulfate. Catalytic polypeptides with molecular masses of about 97 , 74, 36, 29, and 25 kDa were observed in media from young cultures, t hough progressively fewer bands were observed as cultures aged. Based on size estimations of native enzymes with gel exclusion chromatograph y, the 97- and 36-kDa polypeptides were concluded to be subunits of a 245-kDa holoenzyme and the 25-kDa polypeptides were concluded to be su bunits of a second holoenzyme of about 92 kDa. The data were insuffici ent to allow similar assignments for the more ephemeral 74- and 29-kDa polypeptides. The endoglucanases secreted during branch induction by antheridiol or 0.2% peptone comigrated in electrophoretic gels with en zymes secreted during normal assimilative growth. No endoglucanases sp ecific to induced branching were observed.