In vitro photoactivation of chitin syntheses from Phycomyces blakesleanus sporangiophores
DOI:
https://doi.org/10.33885/sf.1987.3.702Abstract
We analyzed the mechanism of photoactivation of chitin
synthetase present in the Phycomyces sporangiophores in stage
IV. The enzyme was partially 'stabilized by addition of sucrose
t o ihe homogenization media, its activity was optimal at pH 7.8,
and it was stimulated by addition of exogenous proteases.
Illumination of cell-free extracts during the chitin synthetase
assays stimulated signi ficantly enzymatic ·activity: an aver ag e
of 75% and 21% in the absence or in the presen~e of trypsin,
respectively. In darkness, low concentrations of Ca+2 bro ught
about a slight activation, but higher concentrations were
inhibitory. Nevertheless, its addition gave rise to high l evels
of stimulation by light. lodo-acetamide inhibited chitin
synthetase activati on by both, light or trypsin. We propose a
working model for the photoactivation of chitin synthetase to
account for these observations
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