Enzymatic mechanisms for the inactivation of luteinizing hormone-releasing hormone (LH-RH).
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Biomedical subjects
Publications and source records attributed to N Marks.
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The pentapeptide pepstatin obtained from culture filtrates of actinomycetes completely inhibited brain acid proteinase (cathepsin D) at exceedingly low concentrations. Among the brain enzymes tested, the effect is specific for acid proteinase because addition of 1000-fold higher concentrations was without effect on neutral proteinase, aminopeptidase, and arylamidases. Pepstatin also inhibits pepsin as tested with hemoglobin or with N-acetylphenylalanyl-L-diiodotyrosine as substrate. Pepstatin must be regarded as the most powerful agent yet described that inhibits intracellular acidic proteolytic enzyme in brain.
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