Primary structure of chum salmon prolactins: occurrence of highly conserved regions.
Primary structure of chum salmon prolactins: occurrence of highly conserved regions.
复制标题
鲑鱼催乳素的一级结构:高度保守区域的出现。
DOI:
10.1016/0003-9861(86)90621-1
复制
发表时间:
1986
影响因子:
3.9
通讯作者:
H. Kawauchi
中科院分区:
文献类型:
--
作者:
A. Yasuda;H. Itoh;H. Kawauchi
The complete amino acid sequence of prolactin from the pituitaries of salmon (Oncorhynchus keta) has been determined. Salmon prolactin comprised two variants, I and II, which were separated by reverse-phase high-performance liquid chromatography. Each variant was reduced,S-carboxymethylated, and then cleaved with cyanogen bromide and enzymes. The resulting fragments were separated by reverse-phase high-performance liquid chromatography, as well as gel filtration, and subjected to sequence analysis by the dansyl-Edman method. Both variants contain 187 amino acid residues with two disulfide linkages at residues 46–160 and 177–187, lack a linkage in the N-terminal portion of mammalian prolactins, and differ from each other by the replacement of only four amino acid residues. Salmon prolactin (sPRL) shows 31% sequence identity with ovine prolactin. Moreover, four restricted regions, i.e., sPRL (3–21), (46–60), (68–83), and (160–178), encompass this significant conservatism between the teleost and the mammalian hormone, with identities of 47, 87, 62, and 68%, respectively. Such considerable identity between these distant phylogenic species strongly suggests that these regions may be responsible for the biological activity of prolactin.