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Isolation and partial characterization of a Mr 32,000 protein with inhibin activity from porcine follicular fluid.

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, res...

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Bibliografiska uppgifter
Huvudupphovsmän: Ling, N, Ying, S Y, Ueno, N, Esch, F, Denoroy, L, Guillemin, R
Materialtyp: Artigo
Språk:Inglês
Publicerad: 1985
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Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC390820/
https://ncbi.nlm.nih.gov/pubmed/3864157
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