Abstract
A neutral endopeptidase which degrades luteinizing hormone-releasing hormone (LH-RH, <GLu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-GLy-NH2) has been purified 900-fold from extracts of bovine anterior pituitary. This Ca2+-independent enzyme of 83 000 molecular weight (as estimated by gel filtration) cleaves LH-RH (KM = 180 microM) at the Tyr5-Gly6-His2-Trp3 bonds. Its activity is inhibited by the SH-reactive agents N-ethylmaleimide and p-(chloromercuri)benzoate but not by the OH-reactive agent diisopropyl fluorophosphate. Hydrolysis of the fluorogenic chymotrypsin substrate glutarkyl-Gly-Gly-Phe-beta-naphthylamide by this endopeptidase could not be detected. These properties differentiate the endopeptidase from chymotrypsin and from a glutaryl-Gly-Gly-Phe-beta-naphthylamide hydrolyzing activity of high molecular weight, which has been isolated from the same tissue and also hydrolyzes internal bonds of LH-RH.
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