Thymidine phosphorylase activity associated with platelet-derived endothelial cell growth factor

Tomoyuki Sumizawa, Tatsuhiko Furukawa, Misako Haraguchi, Akihiko Yoshimura, Akira Takeyasu, Minoru Ishizawa, Yuji Yamada, Shin Ichi Akiyama

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167 Citations (Scopus)


Partial complementary DNA (cDNA) for thymidine phosphorylase (dThdPase) was cloned by means of a polymerase chain reaction. There was complete sequence identity between the amino acid sequence deduced from the nucleotide sequence of a clone (288 nucleotides) and the residues of platelet-derived endothelial cell growth factor (PD-ECGF). The amino acid sequence of all four peptide fragments from purified human dThdPase could be aligned with that of PD-ECGF. Our data indicate that residues 125-244 of PD-ECGF are identical to the sequence of human dThdPase. The molecular weights of human dThdPase and recombinant PD-ECGF (rPD-ECGF) that lacks 10 amino acids at the amino terminal were 55 and 52 kDa, respectively. Anti-PD-ECGF antibody recognized dThdPase, and anti-dThdPase antibody recognized rPD-ECGF. rPD-ECGF had dThdPase activity and its specific activity was similar to that of purified human dThdPase. dThdPase activity and molecules were detected in COS cells transfected with human PD-ECGF cDNA, but not in nontransfected cells. The sizes of PD-ECGF and dThdPase in the transfected COS cells were identical. These data suggest that human dThdPase is identical to PD-ECGF.

Original languageEnglish
Pages (from-to)9-14
Number of pages6
JournalJournal of biochemistry
Issue number1
Publication statusPublished - 1993 Jul
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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