Luteinizing hormone. The primary structures of the beta-subunit from bovine and porcine species.
Luteinizing hormone. The primary structures of the beta-subunit from bovine and porcine species.
复制标题
黄体生成素。
DOI：
10.1111/j.1432-1033.1973.tb03121.x
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发表时间：
1973
期刊：
影响因子：
--
通讯作者：
G. Hennen
中科院分区：
文献类型：
--
作者：
G. Maghuin;G. Hennen
测定了牛和猪促黄体生成素β亚基的119个氨基酸的序列，在这些物种之间观察到17个氨基酸替换。观察到猪β-亚基一级结构的变异性，因为位置10被N-乙酰基和谷氨酰残基占据。猪和牛β多肽链均未检测到游离氨基末端残基，且均表现出羧基末端异质性。讨论了不同物种的促黄体激素β亚基和牛促甲状腺激素β亚基的同源性，因为这两种激素的亚基可以与相似的α亚基联合收割机结合。
The sequences of the 119 amino acids of bovine and porcine luteinizing hormone β‐subunits were determined, 17 amino acid replacements being observed between these species. Variability in the primary structure was observed for porcine β‐subunit, in that position 10 is occupied by both arginyl and glutamyl residues. No free amino terminal residue was detected for both porcine and bovine β‐polypeptide chains and both exhibited carboxy‐terminal heterogeneity. The homology of the β‐subunits of luteinizing hormone from various species and the β‐subunit of the bovine thyroid‐stimulating hormone is discussed as the subunit of both hormones can combine with a similar α‐subunit.