Abstract
1. Met-enkephalin is degraded by peptidases present in the hemolymph fluid and hemocyte membrane suspension of Mytilus edulis. Degradation of Met-enkephalin is rapid in the fluid and slower in the membrane. 2. Aminopeptidase activity is bestatin sensitive in hemocyte membrane and highest in the fluid of the hemolymph, which appears to have a component which is insensitive to inhibitor. 3. ACE activity is found only in the fluid of the hemolymph. 4. Carboxypeptidase and NEP (CD10: "enkephalinase") are membrane bound and the former appears to predominate. Phosphoramidon inhibits not only NEP, as expected, but the invertebrate carboxypeptidase as well.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Aminopeptidases / antagonists & inhibitors
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Aminopeptidases / blood*
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Animals
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Bivalvia / metabolism*
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Carboxypeptidases / blood*
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Cell Membrane / enzymology
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Chromatography, High Pressure Liquid
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Enkephalin, Methionine / metabolism*
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Glycopeptides / pharmacology
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Hemocytes / enzymology
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Hemolymph / enzymology*
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Leucine / analogs & derivatives
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Leucine / pharmacology
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Membrane Proteins / blood*
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Molecular Sequence Data
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Neprilysin / blood*
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Peptidyl-Dipeptidase A / blood*
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Substrate Specificity
Substances
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Glycopeptides
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Membrane Proteins
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Enkephalin, Methionine
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Carboxypeptidases
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Aminopeptidases
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Peptidyl-Dipeptidase A
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Neprilysin
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Leucine
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ubenimex
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phosphoramidon