Stability of several LHRH antagonists against proteolytic enzymes and identification of degradation products by mass spectrometry.
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.
Braun
K
K
Institute of Biochemistry, University of Technology Dresden, Germany. Karin.Braun@chemie.tu-dresden.de
Kuhl
P
P
Bernd
M
M
Kutscher
B
B
D002853:Chromatography, Liquid; D010450:Endopeptidases / Q000737:chemistry*; D007987:Gonadotropin-Releasing Hormone / Q000031:analogs & derivatives* / Q000037:antagonists & inhibitors* / Q000737:chemistry; D006727:Hormone Antagonists / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D009842:Oligopeptides / Q000737:chemistry; D013379:Substrate Specificity
C421984:D-21744; C421983:D-21973; D006727:Hormone Antagonists; D009842:Oligopeptides; D007987:Gonadotropin-Releasing Hormone; C084350:antarelix; D010450:Endopeptidases; C062876:cetrorelix