Stability of several LHRH antagonists against proteolytic enzymes and identification of degradation products by mass spectrometry

K Braun; P Kuhl; M Bernd; B Kutscher

Stability of several LHRH antagonists against proteolytic enzymes and identification of degradation products by mass spectrometry

Pharmazie. 2001 Jan;56(1):45-9.

Authors

K Braun¹, P Kuhl, M Bernd, B Kutscher

Affiliation

¹ Institute of Biochemistry, University of Technology Dresden, Germany. Karin.Braun@chemie.tu-dresden.de

PMID: 11210667

Abstract

In this study stabilities of several LHRH antagonists against proteolytic enzymes are compared. For the enzymatic tests 15 proteases which differ in both substrate specificity and pH optimum were selected. The cyclic and two linear antagonists proved to be extraordinarily stable against the enzymes used over an incubation time of 50 h. Some degradation products were identified by high-performance liquid chromatography combined with mass spectrometry.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chromatography, Liquid
Endopeptidases / chemistry*
Gonadotropin-Releasing Hormone / analogs & derivatives*
Gonadotropin-Releasing Hormone / antagonists & inhibitors*
Gonadotropin-Releasing Hormone / chemistry
Hormone Antagonists / chemistry
Hydrogen-Ion Concentration
Mass Spectrometry
Oligopeptides / chemistry
Substrate Specificity

Substances

D-21744
D-21973
Hormone Antagonists
Oligopeptides
Gonadotropin-Releasing Hormone
antarelix
Endopeptidases
cetrorelix