STRUCTURE OF HUMAN LUTEINIZING-HORMONE BETA SUBUNIT - EVIDENCE FOR A RELATED CARBOXYL-TERMINAL SEQUENCE AMONG CERTAIN PEPTIDE-HORMONES

被引：40
作者：
KEUTMANN, HT
WILLIAMS, RM
RYAN, RJ
机构：
[1] HARVARD UNIV,MASSACHUSETTS GEN HOSP,SCH MED,BOSTON,MA 02114
[2] MAYO MED SCH,DEPT MOLEC MED,ROCHESTER,MN 55901
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 90卷 / 03期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1016/0006-291X(79)91904-1
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Amino acid sequence analysis of human luteinizing hormone (lutropin) beta subunit has been carried out in order to reconcile several discrepancies apparent in previously published structures. Our sequence coincides closely with that proposed originally by Shome and Parlow (J.Clin.Endocr.Metab. 36, 618-621, 1973). However, we found a unique solution to the carboxyl-terminal region (-Thr-Cys-Asp-His-Pro-Gln-OH) which is closely homologous with the corresponding segment of hCG and the animal LH beta subunits. The C-terminal three residues appear in closely similar sequences at the C-termini of several other peptide hormones. This suggests a primitive genomic relationship with conservation of this region during evolution of these otherwise divergent polypeptides. © 1979.
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页码：842 / 848
页数：7
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