Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell.

@article{Sugino1993MolecularHO,
  title={Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell.},
  author={Kentaro Sugino and Nobuyuki Kurosawa and Tatsuji Nakamura and Koji Takio and Shunichi Shimasaki and Nicholas Ling and Koiti Titani and Hiromu Sugino},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 21},
  pages={15579-87}
}
Follistatin (FS), an activin-binding protein, is a monomer derived from two polypeptide core sequences of 315 (FS-315) and 288 (FS-288) amino acids originated from alternatively spliced mRNA. To define the structural heterogeneity of native FS, we purified six molecular forms of FS from porcine ovaries. Protein chemical analysis revealed that the structural differences among the six isoforms were caused by truncation of the carboxyl-terminal region and/or the presence of carbohydrate chains… CONTINUE READING
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