Hook V Y, Mezey E, Fricker L D, Pruss R M, Siegel R E, Brownstein M J
Proc Natl Acad Sci U S A. 1985 Jul;82(14):4745-9. doi: 10.1073/pnas.82.14.4745.
Specific rabbit antisera against purified bovine pituitary carboxypeptidase processing enzyme (which has also been referred to as "enkephalin convertase") have been prepared and characterized. The antisera recognized both the purified soluble and the membrane-bound forms of the enzyme with equal affinity, suggesting that these two forms of the enzyme may possess many regions of structural homology. Since the antisera did not crossreact with carboxypeptidases B, N, A, Y, and P, the carboxypeptidase processing enzyme may be a structurally distinct form of carboxypeptidase. Carboxypeptidase immunostaining, as seen by light microscopy, was found throughout the rat brain and in bovine adrenal medulla, reflecting the widespread distribution of neuropeptides. Electron microscopic immunocytochemistry of rat paraventricular nucleus and other brain areas showed that the enzyme was present in some dendrites and nerve terminals, which contain storage vesicles. These findings support the hypothesis that this carboxypeptidase is involved in the processing of many peptide hormone precursors.
已经制备并鉴定了针对纯化的牛垂体羧肽酶加工酶（也被称为“脑啡肽转化酶”）的特异性兔抗血清。这些抗血清以相同的亲和力识别该酶的纯化可溶性形式和膜结合形式，这表明该酶的这两种形式可能具有许多结构同源区域。由于这些抗血清与羧肽酶B、N、A、Y和P不发生交叉反应，因此羧肽酶加工酶可能是一种结构上独特的羧肽酶形式。通过光学显微镜观察发现，羧肽酶免疫染色遍布大鼠脑和牛肾上腺髓质，这反映了神经肽的广泛分布。大鼠室旁核和其他脑区的电子显微镜免疫细胞化学显示，该酶存在于一些含有储存小泡的树突和神经末梢中。这些发现支持了这样一种假说，即这种羧肽酶参与了许多肽激素前体的加工过程。
