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

@article{Ling1985IsolationAP,
  title={Isolation and partial characterization of a Mr 32,000 protein with inhibin activity from porcine follicular fluid.},
  author={Nicholas Ling and S Y Ying and Naoto Ueno and Fred S. Esch and Luc Denoroy and Roger Guillemin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1985},
  volume={82 21},
  pages={7217-21}
}
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… CONTINUE READING

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