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  • Title: A peptidyl alpha-amidation activity in chromaffin granules of bovine adrenal medulla.
    Author: Bastiaensen E, De Potter W.
    Journal: FEBS Lett; 1989 Feb 27; 244(2):477-80. PubMed ID: 2920841.
    Abstract:
    Peptidyl alpha-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 Cu2+ and ascorbate. The pH maximum for alpha-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.
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