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Carboxypeptidase activity in the insulin secretory granule
Author(s) -
Docherty Kevin,
Hutton John C.
Publication year - 1983
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(83)81065-5
Subject(s) - carboxypeptidase , granule (geology) , biochemistry , enzyme , chemistry , insulin , amino acid , enzyme assay , biology , endocrinology , paleontology
Carboxypeptidase activity was studied in subcellular fractions from a transplantable rat insulinoma and found to be localised principally in the insulin secretory granule. The activity, which was specific for peptide substrates with C‐terminal basic amino acids, appeared to be a single enzyme with M r 54 000. This enzyme differed with respect to size and pH optimum from other basic amino acid‐specific carboxypeptidases, such as carboxypeptidases B and N, and may be a secretory granule‐specific enzyme involved in propolypeptide processing.