JBC, Vol. 254, Issue 1, 50-56, Jan, 1979
Serine proteinases and their inhibitors in Phycomyces blakesleeanus
E. P. Fischer and K. S. Thomson
Three serine proteinases of Phycomyces blakesleeanus were isolated and
characterized. The molecular weights were determined to be 18,000, 22,000,
and 60,000. The proteinases were solubilized by detergent or salt
treatment. Two soluble proteins that specifically inhibit these proteinases
were also isolated and characterized. Both these proteins formed 1:1
complexes with the serine proteinases. A molecular weight of 10,000 was
estimated for both inhibitors. They were found to be present in excess in
the cells. An acid proteinase of Phycomyces was able to take the inhibitor
off a serine proteinase.inhibitor complex. This proteinase was partially
purified. The proteinases and inhibitors of three mutant strains were
partially purified and compared with a standard strain. These mutants
exhibit abnormal growth responses of the sporangiophore to light. Mutant
specific changes of the proteinases and their inhibitors were detected, but
a connection to the behavioral responses could not be demonstrated.