牛脾脏酸性激肽原酶生成激肽的研究。

Studies on the kinin formation by bovine spleen acid kininogenases.

作者信息

Yamafuji K, Watanabe M

出版信息

Adv Exp Med Biol. 1983;156:409-18.

Abstract

The modes of action of acid kininogenase I and II on bovine kininogens were investigated. The pH profile of kinin forming reaction from bradykininogen for each enzyme proved the fact that these enzymes react preferably at acidic condition. Acid kininogenase I produced kinin presumably from nicked HMW kininogen which has bradykinin moiety at the C-terminal, but not from intact HMW or LMW kininogens. Acid kininogenase II could react on any kind of kininogen tested. The peptides produced were purified and subjected to molecular weight determination and also to sequence analysis. Estimated molecular weights were 1,300 and 1,400 for the peptides produced by AK I and 1,900 for the one produced by AK II. N-terminal amino acids were revealed to be methionine, leucine and arginine, respectively.

摘要

研究了酸性激肽原酶I和II对牛激肽原的作用模式。每种酶催化缓激肽原生成激肽的反应的pH曲线证明了这些酶在酸性条件下反应更优这一事实。酸性激肽原酶I可能从在C端含有缓激肽部分的缺口高分子量激肽原产生激肽，但不能从完整的高分子量或低分子量激肽原产生激肽。酸性激肽原酶II可以作用于所测试的任何一种激肽原。所产生的肽段经过纯化，进行分子量测定和序列分析。酸性激肽原酶I产生的肽段估计分子量为1300和1400，酸性激肽原酶II产生的肽段估计分子量为1900。N端氨基酸分别被鉴定为甲硫氨酸、亮氨酸和精氨酸。