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A peptidyl α‐amidation activity in chromaffin granules of bovine adrenal medulla
Author(s) -
Bastiaensen Erik,
De Potter Werner
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80587-3
Subject(s) - adrenal medulla , chromaffin cell , chemistry , medulla , endocrinology , medicine , biochemistry , biology , catecholamine
Peptidyl α‐amidation activity in bovine adrenal medulla has been localized in chromaffin granules by density gradient centrifugation. The activity was found to be both soluble and membrane‐associated. Both enzymatic activities were stimulated by the addition of Cu 2+ and ascorbate. The pH maximum for α‐amidation in the chromaffin granules in pH 8.0–8.5. By gel filtration, the soluble enzyme activity appeared as a protein of approx. 40 kDa. It is suggested that this enzyme is involved in the carboxyl‐terminal amidation of metorphamide, amidorphin and neuropeptide Y.