Metabolism of thyrotropin releasing hormone in brain extracts. Isolation and characterization of an imidopeptidase for histidylprolineamide.
作者： C. Prasad , A. Peterkofsky , T. Matsui
DOI: 10.1016/S0021-9258(17)30242-9
关键词:
摘要: An extract of porcine brain acetone powder incubated with thyrotropin-releasing hormone (TRH; pGlu-His-ProNH2) produces acid TRH (pGlu-His-Pro), histidine, and prolineamide. Fractionation the by DEAE-cellulose chromatography three protein fractions which metabolize TRH. The activity these was characterized using a 3H-label on histidine or proline as well [His-3H]His-ProNH2. Fraction I contains pyroglutamate aminopeptidase II deamidase. III found to contain previously unrecognized enzyme cleaves His-ProNH2 proline. histidylprolineamide imidopeptidase has been characterized. A competition study variety compounds containing suggests that best substrates for free alpha-amino group blocked carboxyl proline, is in His-ProNH2. survey polypeptide hormones indicates many them inhibit activity. kinetic inhibition adrenocorticotropic (1-24) shows noncompetitive. We hypothesize pituitary may stimulate production (cyclo)-His-Pro inhibiting alternate routes metabolism.
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