Taljanidisz J, Stewart L, Smith A J, Klinman J P
Department of Chemistry, University of California, Berkeley 94720.
Biochemistry. 1989 Dec 26;28(26):10054-61. doi: 10.1021/bi00452a026.
A full-length cDNA for dopamine beta-monooxygenase (D beta M) from bovine adrenal glands has been cloned and sequenced. The soluble and membrane-derived forms of D beta M have also been sequenced from their N-termini. While the observed sequences for the soluble protein correspond to those previously reported [Joh, T.H., & Hwang, O. (1986) Ann. N.Y. Acad. Sci. 493, 343-350], the heavy subunit of membrane-derived enzyme is found to contain a unique N-terminus. Alignment of this N-terminus with that deduced from cDNA cloning indicates identity at 22 (and possibly 26) out of 27 residues. This comparison leads us to conclude that the membranous form of bovine D beta M retains an uncleaved N-terminal signal peptide as the source of membrane anchoring.
已克隆并测序了来自牛肾上腺的多巴胺β-单加氧酶（DβM）的全长cDNA。还从其N端对DβM的可溶性形式和膜衍生形式进行了测序。虽然可溶性蛋白的观察序列与先前报道的序列一致[Joh, T.H., & Hwang, O. (1986) Ann. N.Y. Acad. Sci. 493, 343 - 350]，但发现膜衍生酶的重亚基含有独特的N端。将该N端与cDNA克隆推导的N端进行比对，结果显示在27个残基中有22个（可能26个）相同。这种比较使我们得出结论，牛DβM的膜形式保留了一个未切割的N端信号肽作为膜锚定的来源。
