A SPECIFIC ENDOPEPTIDASE, BAEE ESTERASE, IN THE GLANDULAPROSTATICA OF THE MALE REPRODUCTIVE-SYSTEM OF THE SILKWORM, BOMBYX-MORI
A SPECIFIC ENDOPEPTIDASE, BAEE ESTERASE, IN THE GLANDULAPROSTATICA OF THE MALE REPRODUCTIVE-SYSTEM OF THE SILKWORM, BOMBYX-MORI
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DOI：
10.1016/0020-1790(87)90075-8
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发表时间：
1987-01-01
期刊：
影响因子：
--
通讯作者：
OSANAI, M
中科院分区：
文献类型：
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作者：
AIGAKI, T;KASUGA, H;OSANAI, M
精氨酸酯水解酶(BAEEase)是一种特殊的内肽酶。家蚕射精管的下部，也称前列腺区。在雄性生殖腺中，只有前列腺癌被发现含有这种酶。用硫酸铵沉淀法对该酶进行了部分纯化，并对其进行了酶学性质研究。在pH 9.0~9.5范围内，BAEEase活性最高。该酶在25℃、pH 5.0以上非常不稳定。C，但在0.1M KCl存在下仍稳定在pH 4.0。与牛胰酶不同，前列腺BAEEase对BAEE有明显的水解性，对TAME有轻微的水解性，但对TLME无水解性。胰酶抑制剂p-NPGB、亮肽素和止痛剂对该酶有明显的抑制作用，而其他丝氨酸蛋白酶抑制剂、硫醇酶抑制剂和羧基蛋白酶抑制剂则不能抑制该酶的活性。结果表明，前列腺BAEEase可能是一种新的丝氨酸蛋白内切酶，专一性地裂解精氨酸残基C侧的蛋白质。
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.