ISOLATION AND PARTIAL CHARACTERIZATION OF A MR 32,000 PROTEIN WITH INHIBIN ACTIVITY FROM PORCINE FOLLICULAR-FLUID
ISOLATION AND PARTIAL CHARACTERIZATION OF A MR 32,000 PROTEIN WITH INHIBIN ACTIVITY FROM PORCINE FOLLICULAR-FLUID
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DOI：
10.1073/pnas.82.21.7217
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
GUILLEMIN, R
中科院分区：
文献类型：
--
作者：
LING, N;YING, SY;GUILLEMIN, R
通过肝素-Sepharose亲和层析、Sephacryl S-200凝胶过滤和四个反相HPLC步骤，从猪卵泡液中分离到一个Mr为32，000的蛋白质，该蛋白质具有胰蛋白酶活性。分离的分子由分子量分别为18，000和14，000的两条链组成，并通过二硫键结合在一起。氨基酸序列分析表明，Mr18，000链的10个NH2端残基为Ser-Thr-Ala-Pro-Leu-Pro-Trp-Pro-Trp-Ser-，Mr14，000链的10个NH2端残基为Gly-Leu-Glu-Xaa-Asp-Gly-Arg-Thr-Asn-Leu。在大鼠垂体前叶单层培养系统中，这种Mr 32，000蛋白特异性抑制FSH的基础分泌，但不抑制LH的基础分泌，半最大有效剂量为450 pg/ml。
A Mr 32,000 protein with inhibin activity was isolated from porcine follicular fluid by heparin-Sepharose affinity chromatography, gel filtration on Sephacryl S-200, and four reversed-phase HPLC steps. The isolated molecule is composed of two chains having molecular weights of 18,000 and 14,000, respectively, and bound together by disulfide bonds. Amino acid sequence analysis revealed the 10 NH2-terminal residues of the Mr 18,000 chain to be Ser-Thr-Ala-Pro-Leu-Pro-Trp-Pro-Trp-Ser- and those of the Mr 14,000 chain to be Gly-Leu-Glu-Xaa-Asp-Gly-Arg-Thr-Asn-Leu. This Mr 32,000 protein specifically inhibits the basal secretion of FSH, but not that of LH, in the rat anterior pituitary monolayer culture system, with a half-maximal effective dose of 450 pg/ml.