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