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  • Title: Structural characterization of thymidine phosphorylase purified from human placenta.
    Author: Miyadera K, Dohmae N, Takio K, Sumizawa T, Haraguchi M, Furukawa T, Yamada Y, Akiyama S.
    Journal: Biochem Biophys Res Commun; 1995 Jul 26; 212(3):1040-5. PubMed ID: 7626090.
    Abstract:
    Human thymidine phosphorylase (dThdPase) is thought to be identical to an angiogenesis factor, platelet-derived endothelial cell growth factor (PD-ECGF). However, the whole amino acid sequence of dThdPase is still unknown. N-terminal amino acid sequencing of dThdPase isolated from human placenta gave the sequence Ac-AALMTPGTGAPPAPG. Comparison with the sequence predicted from the PD-ECGF cDNA reveals that residues 2-16 of dThdPase are identical to that of PD-ECGF. If dThdPase and PD-ECGF are derived from the same gene, the primary translational product of dThdPase would be processed one amino acid from the translation-initiating methionine residue and Ala-2 acetylated. Since placental and platelet PD-ECGF is reported to be processed at Thr-6 and Ala-11, respectively, and the N-terminal end is not blocked, further study is needed to clarify the reason for this discrepancy and whether the difference in N-terminal sequence affects the physiological function of these molecules.
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