Purification and characterization of thrombopoietin

Takashi Kato*, Kinya Ogami, Yoshihiro Shimada, Akihiro Iwamatsu, Yoshiaki Sohma, Hiromichi Akahori, Kaori Horie, Atsuko Kokubo, Yoko Kudo, Emiko Maeda, Keiko Kobayashi, Hideya Ohashi, Tadashi Ozawa, Hideo Inoue, Kazuo Kawamura, Hiroshi Miyazaki


研究成果: Article査読

249 被引用数 (Scopus)


A thrombopoietic factor, termed thrombopoietin (TPO), was highly purified directly from the plasma of sublethally irradiated 1, 100 rats by measuring the production of megakaryo-cytes from a highly enriched population of rat megakaryocyte progenitor cells (CFU-MK). The rat plasma TPO is a glycoprotein and strongly hydrophobic. The total activity and purification yields obtained were about 29% and 1.49%108, respectively. The amino acid sequences of the two peptide fragments prepared from the purified 19 kDa TPO were analyzed, and used for the cloning of rat and human TPO cDNAs. It was found that the 19 kDa TPO was truncated but comprised at least 163 amino acids. The sequence of human TPO cDNA revealed that the TPO was identical to the c-Mpl ligand. Both rat and human TPOs expressed in COS-1 cells exhibited significant activity toward the CFU-MK in vitro and were active in stimulating platelet production in mice. These results indicate that a thrombopoietic factor originally found in the irradiated rat plasma is a ligand for the rat c-Mpl.

ジャーナルJournal of biochemistry
出版ステータスPublished - 1995 7月

ASJC Scopus subject areas

  • 生化学
  • 分子生物学


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