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- W2074152281 abstract "Thimet peptidase has been purified from rat liver mitochondria and found to share the characteristics of a thiol‐dependent metallo‐endopeptidase previously described for an enzyme in the cytosolic fraction from rat testis: inhibition by EDTA, reactivation by Zn 2+ , requirement of dithiothreitol for maximal and stable activity, and inhibition by N ‐ethylmaleimide. The K i for inhibition by N ‐[1‐(RS)‐carboxy‐3‐phenylpropyl]‐Ala‐Ala‐Phe‐ p ‐aminobenzoic acid is 2.6 μM, 100‐fold higher than the value for the cytosolic form. The mitochondrial form is not inhibited by antisera against the cytosolic form, and the two forms of the enzyme show quantitative differences in substrate specificity. The name thimet peptidase II is suggested for the enzyme from rat mitochondria." @default.
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- W2074152281 date "1990-05-07" @default.
- W2074152281 modified "2023-10-14" @default.
- W2074152281 title "A distinct thimet peptidase from rat liver mitochondria" @default.
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- W2074152281 doi "https://doi.org/10.1016/0014-5793(90)80771-a" @default.
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