The protease purifiedjkom hepatopancreas of shrimp, Penaeus orientalis, had high proteolytic activity in the p H range of 7.0 to 9.5. Temperature optimum for hydrolysis of casein was 70C. The protease was stable at neutral and alkaline pH and unstable at acidic pH. The apparent Michaelis-Menten constant (KJ and the turnover number (V,J of the protease on hydrolysis of N-CBZ-L-tyrosine p-nitrophenyl ester (CBZ-Tyr-NE) and N-CBZ-L-phenylalanine p-nitrophenyl ester (CBZ-Phe-NE) were similar, however, those for N-CBZ-L-cysteine p-nitrophenyl ester (CBZ-Cys-NE) were difjerent. K, and Vmat for hydrolysis of casein by the protease were determined to be 0.31% and 5.21s-', respectively. The N-terminal sequence of the protease showed higher homology with the collagenase of crab and trypsins from crustacea. Myosin heavy chain (MHC) was the primary substrate during proteolysis with the protease. Actin/tropomyosin were degraded progressively during 2 h incubation but to a lesser extent than MHC.

During laparotomy for a huge parovarian cyst, unusually large bilateral lobulated ovarian cysts were noted. And lobulated ovary is one of the rarest gynecologic abnormalities. Although obesity and hirsutism were absent and the results of the endocrine test were within normal range, polycystic ovarian disease was highly suspected due to the pathologic findings and elevated LH/FSH ratio.

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