Liston D, Böhlen P, Rossier J
J Neurochem. 1984 Aug;43(2):335-41. doi: 10.1111/j.1471-4159.1984.tb00905.x.
The primary sequence of adrenal proenkephalin was recently deduced from the structure of the cloned cDNA that codes for this protein. Several enkephalin-containing proteins with molecular weights between 8,000 and 20,000 daltons were purified from the bovine adrenal medulla. These proteins appear to represent intermediates in the processing of proenkephalin into physiologically active opioid peptides. While the concentrations of these large processing intermediates in the adrenal medulla are quite high, similar proteins have not yet been shown to be present in brain, and there is some question as to whether the brain synthesizes an enkephalin precursor similar to adrenal proenkephalin. We report here the purification from bovine caudate nucleus of synenkephalin, the N-terminal fragment of adrenal proenkephalin. The amino acid composition of synenkephalin indicates that the protein represents residues 1-70 of adrenal proenkephalin. Thus the brain and adrenal glands appear to utilize a similar precursor for enkephalin biosynthesis.
肾上腺前脑啡肽原的一级序列最近已从编码该蛋白质的克隆cDNA结构中推导出来。从牛肾上腺髓质中纯化出了几种分子量在8000至20000道尔顿之间的含脑啡肽蛋白。这些蛋白质似乎代表了前脑啡肽原加工成生理活性阿片肽过程中的中间体。虽然这些大的加工中间体在肾上腺髓质中的浓度相当高，但尚未证明脑中存在类似的蛋白质，并且关于脑是否合成类似于肾上腺前脑啡肽原的脑啡肽前体存在一些疑问。我们在此报告从牛尾状核中纯化出的突触脑啡肽，它是肾上腺前脑啡肽原的N端片段。突触脑啡肽的氨基酸组成表明该蛋白质代表肾上腺前脑啡肽原的1至70位残基。因此，脑和肾上腺似乎利用相似的前体进行脑啡肽的生物合成。
