促黄体激素释放激素（LHRH）拮抗剂安替肽对细胞表面肽酶的代谢稳定性。

Metabolic stability of the LHRH antagonist antide to cell-surface peptidases.

作者信息

Medeiros M dos S, Turner A J, Ljungqvist A, Folkers K

机构信息

Department of Biochemistry, University of Leeds, UK.

出版信息

Biochem Biophys Res Commun. 1991 Apr 15;176(1):25-30. doi: 10.1016/0006-291x(91)90884-a.

DOI:10.1016/0006-291x(91)90884-a

PMID:2018520

Abstract

The susceptibility to hydrolysis of LHRH and the decapeptide analogue Antide has been compared. The hydrolysis of LHRH by pig kidney brush border membranes is inhibited by phosphoramidon (I50 = 5.6 nM) implicating endopeptidase-24.11 in the initiation of hydrolysis. Under conditions in which LHRH is fully degraded by brush border membranes, Antide was completely resistant to hydrolysis. Similar results were obtained with purified preparations of both endopeptidase-24.11 and angiotensin converting enzyme. These data confirm that the remarkable duration of action of Antide is due principally to its stability to hydrolysis by cell-surface peptidases.

摘要

已对促黄体激素释放激素（LHRH）和十肽类似物Antide的水解敏感性进行了比较。磷酰胺（半数抑制浓度I50 = 5.6 nM）可抑制猪肾刷状缘膜对LHRH的水解，这表明内肽酶-24.11参与了水解起始过程。在刷状缘膜可使LHRH完全降解的条件下，Antide对水解完全具有抗性。用纯化的内肽酶-24.11和血管紧张素转换酶制剂也获得了类似结果。这些数据证实，Antide作用持续时间显著主要是由于其对细胞表面肽酶水解的稳定性。