Docherty K, Hutton J C
FEBS Lett. 1983 Oct 3;162(1):137-41. doi: 10.1016/0014-5793(83)81065-5.
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 Mr 54000. 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.
对可移植大鼠胰岛素瘤的亚细胞组分中的羧肽酶活性进行了研究，发现其主要定位于胰岛素分泌颗粒中。该活性对具有C端碱性氨基酸的肽底物具有特异性，似乎是一种分子量为54000的单一酶。这种酶在大小和最适pH方面与其他碱性氨基酸特异性羧肽酶（如羧肽酶B和N）不同，可能是一种参与前胰岛素原加工的分泌颗粒特异性酶。
