Dissociation of chitosomes from Mucor rouxii by BRIJ 36T
DOI:
https://doi.org/10.33885/sf.1992.3.784Abstract
Incubation of partially purified chitosomes from yeast
cells of H. rouxii with the non-ionic detergent Brij 36T released chitia fibrils following incubation with substrate and activators
of ch~tin synthetase. Activity of dissociated chitin synthetase
was dependent on the presence of phosph~tidylinositol and, as
that of native chitosomes, on activation by an exogenous
protease. On the basis of the morpholoqical and biochemical
characteristics of these particles it is proposed that they are
equivalent to the 165 subunits released from purified chitosomes
following incubation with digitonin.
a population of smaller particles with chitin synthetase activity
which were further purified by molecular weight exclusion
chromatography in a Bio-Gel A-0.5m column. Electron microscopy of
negatively stained samples of most active fractions eluting from
the column revealed the presence of tsodiametric particles, 10-17
nm in diameter, with the ability to synthesize short and thick
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