Capra J D, Kehoe J M, Kotelchuck D, Walter R, Breslow E
Proc Natl Acad Sci U S A. 1972 Feb;69(2):431-4. doi: 10.1073/pnas.69.2.431.
The sequence of the first 50 amino-acid residues of bovine neurophysin-I was determined. A comparison of this sequence with that of the 97-residue bovine neurophysin-II and the 92-residue porcine neurophysin-I molecules reveals a high degree of homology among these proteins. It is suggested that the binding site of neurophysin proteins for neurohypophyseal hormones is located in the middle portion of these molecules, where their sequences are virtually identical. The sequence data, as well as the occurrence of at least two neurophysins in both the pig and the cow, suggest that each species inherited at least two structural genes controlling the synthesis of these proteins. The most striking finding in the study was the observation of internal sequence homologies within the neurophysins. This result implies that these molecules arose by way of a series of partial gene duplications of a primitive gene that coded for a smaller ancestral protein.
已确定牛神经垂体素-I前50个氨基酸残基的序列。将该序列与97个残基的牛神经垂体素-II以及92个残基的猪神经垂体素-I分子的序列进行比较,发现这些蛋白质之间具有高度同源性。有人提出,神经垂体素蛋白与神经垂体激素的结合位点位于这些分子的中部,在那里它们的序列几乎相同。序列数据以及猪和牛中至少存在两种神经垂体素,表明每个物种至少继承了两个控制这些蛋白质合成的结构基因。该研究中最引人注目的发现是观察到神经垂体素内部的序列同源性。这一结果意味着这些分子是由编码较小祖先蛋白的原始基因的一系列部分基因复制产生的。