The Activation of α-Chymotrypsinogen with Proteinase of Streptomyces griseus

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Abstract
It was found that proteinase produced by Str. griseus can activate α-chymotrypsinogen The enzyme which was activated by a limited proteolysis with Str. proteinase, in the presence of β-phenylpropionate was homogeneous on column chromatography, centrifugal sedimentation pattern and paper electrophoresis. This enzyme is called σ-chymotrypsin. Sigma-chymotrypsin has almost the same enzymatic properties (specific activity, Km, Ki) as these of π-chymotrypsin and is quite similar in the secondary and tertiary structure. N-terminal and C-terminal amino acids of σ-chymotrypsin were examined and it was found N-terminal amino acid is isoleucine. Both lysine and arginine were found to be C-terminal amino acids. It was suggested that σ-chymotrypsin is not homogeneous and the activation mechanism with Str. proteinase is somewhat different from that of tryptic activation. A schema of Str. proteinase activation is proposed and the activation mechanism is discussed.

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