HUMAN SEMINAL ALPHA-INHIBINS - ISOLATION, CHARACTERIZATION, AND STRUCTURE
HUMAN SEMINAL ALPHA-INHIBINS - ISOLATION, CHARACTERIZATION, AND STRUCTURE
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DOI:
10.1073/pnas.82.12.4041
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发表时间:
1985-01-01
影响因子:
11.1
通讯作者:
CHUNG, D
中科院分区:
文献类型:
--
作者:
LI, CH;HAMMONDS, RG;CHUNG, D
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.