A specific endopeptidase baee esterase in the glandula prostatica of the male reproductive system of the silkworm bombyx mori

Aigaki, T.; Kasuga, H.; Osanai, M.

Insect Biochemistry 17(2): 323-328


DOI: 10.1016/0020-1790(87)90075-8
Accession: 004629419

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A specific endopeptidase, arginine ester-hydrolyzing enzyme (BAEEase), was demonstrated in the glandula (g.) prostatica, the lower region of the ejaculatory duct of the silkworm, Bombyx mori. Of the male reproductive glands, only the g. prostatica was found to contain this enzyme. The enzyme was partially purified by ammonium sulfate precipitation and characterized enzymologically. The BAEEase activity was maximal at pH 9.0-9.5. The enzyme was very labile above pH 5.0 at 25.degree. C, but was still stabilized at pH 4.0 by the presence of 0.1 M KCl. Unlike bovine trypsin, prostatic BAEEase showed marked hydrolytic activity on BAEE, and slight activity on TAME, but none on TLME. The trypsin inhibitors, p-NPGB, leupeptin and antipain, markedly inhibited the enzyme activity, but other serine protease inhibitors, thiol protease inhibitors and a carboxyl protease inhibitor were not inhibitory. The results indicate that prostatic BAEEase is probably a new endopeptidase of the serine protease group that specifically cleaves protein on the C-side of arginine residues.