被内肽酶3.4.24.11切割后的心房钠尿肽的生物活性
The biological activity of atrial natriuretic factor cleaved by endoprotease 3.4.24.11.
作者信息
Ghai R D, Webb R L, Sonnenberg J L, Sakane Y, Ghai G
机构信息
Research Department, CIBA-GEIGY Corporation, Summit, New Jersey 07901.
出版信息
J Enzyme Inhib. 1991;4(3):267-72. doi: 10.3109/14756369109035850.
PMID:1645400
Abstract
Ring cleavage of atrial natriuretic peptide (ANF) between Cys7 and Phe8 by endoprotease 3.4.24.11 yields X-ANF. Since endoprotease 3.4.24.11 may contribute to ANF metabolism in vivo, the present study determined if X-ANF exhibits reduced biological activity in comparison to the parent molecule.
摘要
心房利钠肽（ANF）经内肽酶3.4.24.11在半胱氨酸7和苯丙氨酸8之间进行环裂解后产生X-ANF。由于内肽酶3.4.24.11可能在体内参与ANF的代谢，本研究确定了与母体分子相比，X-ANF是否表现出降低的生物活性。
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