三磷酸间型霉素作为参与鸟苷酸环化酶激活的ATP结合位点的探针。

Formycin triphosphate as a probe for the ATP binding site involved in the activation of guanylate cyclase.

作者信息

Chang C H, Yu Z N, Song D L

机构信息

Department of Medicine, Case Western Reserve University, Cleveland, OH 44106.

出版信息

Eur J Pharmacol. 1992 Oct 1;227(2):229-31. doi: 10.1016/0922-4106(92)90133-g.

DOI:10.1016/0922-4106(92)90133-g

PMID:1358664

Abstract

Formycin A triphosphate (FTP), a fluorescent analog of ATP, slightly increased basal guanylate cyclase activity, but significantly potentiated guanylate cyclase activity stimulated by atrial natriuretic factor (ANF) in rat lung membranes. FTP potentiated ANF-stimulated guanylate cyclase activity with an EC50 at about 90 microM and inhibited ATP-stimulated guanylate cyclase activity with an IC50 at about 100 microM. These results indicate that FTP binds more tightly than ATP for the same binding site. Therefore, FTP would be an excellent tool for studying the ATP binding site.

摘要

三磷酸间型霉素A（FTP）是一种ATP的荧光类似物，它能轻微增加基础鸟苷酸环化酶活性，但能显著增强大鼠肺膜中由心房利钠因子（ANF）刺激的鸟苷酸环化酶活性。FTP增强ANF刺激的鸟苷酸环化酶活性，其半数有效浓度（EC50）约为90微摩尔，抑制ATP刺激的鸟苷酸环化酶活性，其半数抑制浓度（IC50）约为100微摩尔。这些结果表明，对于相同的结合位点，FTP比ATP结合更紧密。因此，FTP将是研究ATP结合位点的极佳工具。