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T-激肽由组织蛋白酶E样蛋白酶和72 kDa蛋白酶连续切割,从T-激肽原中释放出来。

T-kinin is released from T-kininogen by consecutive cleavage by cathepsin E-like proteinase and 72 kDa proteinase.

作者信息

Sakamoto W, Yoshikawa K, Yokoyama A, Kohri M

出版信息

Biochim Biophys Acta. 1986 Dec 10;884(3):607-9. doi: 10.1016/0304-4165(86)90216-3.

Abstract

Using highly purified T-kininogen and cathepsin E-like proteinase and 72 kDa proteinase in rat spleen, the release of T-kinin from T-kininogen was found to occur by consecutive cleavage by cathepsin E-like proteinase and 72 kDa proteinase. 72 kDa proteinase seems to be serine proteinase, because it was completely inhibited by diisopropyl fluorophosphate but not by pepstatin, leupeptin and bestatin.

摘要

使用高度纯化的T-激肽原、类组织蛋白酶E样蛋白酶和大鼠脾脏中的72 kDa蛋白酶,发现T-激肽从T-激肽原的释放是通过类组织蛋白酶E样蛋白酶和72 kDa蛋白酶的连续切割而发生的。72 kDa蛋白酶似乎是丝氨酸蛋白酶,因为它完全被氟磷酸二异丙酯抑制,而不被胃蛋白酶抑制剂、亮抑酶肽和抑氨肽酶抑制。

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