Document Detail

Isolation and partial characterization of a Mr 32,000 protein with inhibin activity from porcine follicular fluid.
MedLine Citation:
PMID:  3864157     Owner:  NLM     Status:  MEDLINE    
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.
N Ling; S Y Ying; N Ueno; F Esch; L Denoroy; R Guillemin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  82     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1985 Nov 
Date Detail:
Created Date:  1985-12-05     Completed Date:  1985-12-05     Revised Date:  2010-09-13    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7217-21     Citation Subset:  IM    
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MeSH Terms
Amino Acid Sequence
Chromatography, Affinity
Chromatography, Gel
Chromatography, High Pressure Liquid
Inhibins / isolation & purification*,  pharmacology
Molecular Weight
Pituitary Gland, Anterior / drug effects
Grant Support
Reg. No./Substance:

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