Membrane bound pituitary metalloendopeptidase: Apparent identity to enkephalinase |
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Authors: | June Almenoff Sherwin Wilk Marian Orlowski |
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Institution: | Department of Pharmacology, Mount Sinai School of Medicine of the City University of New York, New York, NY 10029 USA |
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Abstract: | A membrane bound zinc-metalloendopeptidase from bovine pituitaries with a specificity toward bonds on the amino side of hydrophobic amino acids, cleaves Met- and Leu-enkephalin at the Gly-Phe bond, releasing Phe-Met and Phe-Leu respectively. The enzyme also hydrolyzes bonds on the amino side of hydrophobic amino acids in oxytocin, bradykinin, neurotensin and several synthetic substrates. A free carboxyl group on a dipeptide C-terminal to the hydrolyzed bond is not a requirement for activity. The enzyme is also present in brain membrane fractions. The regional distribution of this enzyme in brain, its specificity toward natural and synthetic substrates, and its sensitivity to inhibitors, suggest that the enzyme is identical to an activity referred to as “enkephalinase”, which has been described as dipeptidyl carboxypeptidase. The data show that the enzyme is an endopeptidase with a specificity similar to that of a group of microbial proteases, one of which is thermolysin. |
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Keywords: | DFP diisopropylfluorophosphate Cbz N-benzyloxycarbonyl 2NA naphthylamide or 2-naphthylamine 2 naphthylamide or 2-naphthylamine 4Me2NA 4-methoxynaphthylamide Bz α-N-benzoyl HPLC high pressure liquid chromatography |
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