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- W7034075 abstract "Summary We have characterized two distinct brain enzymatic activities which hydrolyze Leu-enkephalin (Leu-Enk). One, a puromycin-sensitive aminopeptidase, fails to cleave the enkephalin analog (D-Ala2)Met-Enk amide, Its specific activity is reduced upon purification of synaptosomal membranes. The second enzyme is a particulate endopeptidase cleaving Leu-Enk at the Gly-Phe peptide bond (Ksbm 2.2×10-5M) to yield Tyr-Gly-Gly and Phe-Leu. (D-Ala2)Met-Enk amide is hydrolyzed by this enzyme although at a lower rate compared to that of Leu-Enk. The endopeptidase cosediments with the synaptosomal membranes. It can be released from the membranes into the high-speed supernatant by the use of Triton X-100. In contrast to the aminopeptidase, the endopeptidase is not inhibited by puromycin or mercurybenzoate but is effectively inhibited by barbiturates." @default.
- W7034075 created "2016-06-24" @default.
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- W7034075 date "1980-01-01" @default.
- W7034075 modified "2023-09-23" @default.
- W7034075 title "DEGRADATION OF ENKEPHALIN BY TWO BRAIN ENZYMATIC ACTIVITIES" @default.
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- W7034075 doi "https://doi.org/10.1016/b978-0-08-025488-3.50092-1" @default.
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