Purification and partial characterization of CD9 antigen of human platelets

@article{Higashihara1990PurificationAP,
  title={Purification and partial characterization of CD9 antigen of human platelets},
  author={M. Higashihara and K. Takahata and Y. Yatomi and K. Nakahara and K. Kurokawa},
  journal={FEBS Letters},
  year={1990},
  volume={264}
}
  • M. Higashihara, K. Takahata, +2 authors K. Kurokawa
  • Published 1990
  • Chemistry, Medicine
  • FEBS Letters
  • CD9 antigen (p24) was purified from human platelets and partially characterized. The yield was 75 μg from 10 units of platelet concentrates. p24 (38 000 copies/platelet) has intramolecular disulfide bond(s) and, in SDS‐PAGE, consists of major 24‐kDa molecule and minor 26‐ to 31‐kDa molecules. The N‐terminal sequence of p24, PVKGOTKXIKYLLFGFNFIF, indicates that the protein has not previously been characterized and amino terminus (position 12–20) is hydrophobic. 
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