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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.
E P Fischer, and
K S Thomson
September 1995,
Current genetics,
E P Fischer, and
K S Thomson
May 1982,
The Biochemical journal,
E P Fischer, and
K S Thomson
January 2003,
Acta biochimica Polonica,
E P Fischer, and
K S Thomson
June 1975,
Genetical research,
E P Fischer, and
K S Thomson
June 1948,
Helvetica chimica acta,
E P Fischer, and
K S Thomson
December 1975,
Experimental cell research,
E P Fischer, and
K S Thomson
February 1979,
Biochemical and biophysical research communications,
E P Fischer, and
K S Thomson
December 1954,
Archives of biochemistry and biophysics,
E P Fischer, and
K S Thomson
July 1988,
Biochimica et biophysica acta,
E P Fischer, and
K S Thomson
May 1954,
The Biochemical journal,
