人精液α抑制素：分离、特性及结构
Human seminal alpha inhibins: isolation, characterization, and structure.
作者信息
Li C H, Hammonds R G, Ramasharma K, Chung D
出版信息
Proc Natl Acad Sci U S A. 1985 Jun;82(12):4041-4. doi: 10.1073/pnas.82.12.4041.
Abstract
Two additional peptides with inhibin-like activity have been isolated from human seminal plasma. One consists of 52 amino acids and the other, 92 amino acids. They are designated alpha-inhibin-52 and alpha-inhibin-92. Sequence analyses show that the NH2-terminal 31 amino acids of alpha-inhibin-52 are identical to the structure of the inhibin-like peptide previously reported [ILP-(1-31), now designated alpha-inhibin-31], and the COOH-terminal 52 amino acids of alpha-inhibin-92 are identical to the structure of alpha-inhibin-52. The amino acid sequence of alpha-inhibin-92 is: (sequence in text) Bioassay data in mouse pituitaries in vitro show that alpha-inhibin-52 is 3.4 times more active and alpha-inhibin-92 is greater than 40 times more active than alpha-inhibin-31 in suppressing follitropin-release. Radioimmunoassay data indicate that alpha-inhibin-52 and alpha-inhibin-92 have only 60% immunoreactivity.
摘要
已从人精浆中分离出另外两种具有抑制素样活性的肽。一种由52个氨基酸组成，另一种由92个氨基酸组成。它们被命名为α-抑制素-52和α-抑制素-92。序列分析表明，α-抑制素-52的NH2末端31个氨基酸与先前报道的抑制素样肽的结构相同[ILP-(1-31)，现命名为α-抑制素-31]，α-抑制素-92的COOH末端52个氨基酸与α-抑制素-52的结构相同。α-抑制素-92的氨基酸序列为：（文本中的序列）体外小鼠垂体生物测定数据表明，在抑制促卵泡激素释放方面，α-抑制素-52的活性是α-抑制素-31的3.4倍，α-抑制素-92的活性比α-抑制素-31高40倍以上。放射免疫测定数据表明，α-抑制素-52和α-抑制素-92的免疫反应性仅为60%。
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