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Structural characterization of thymidine phosphorylase purified from human placenta.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Miyadera K,Dohmae N,Takio K,Sumizawa T,Haraguchi M,Furukawa T,Yamada Y,Akiyama S

doi

10.1006/bbrc.1995.2074

subject

Has Abstract

pub_date

1995-07-26 00:00:00

pages

1040-5

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X85720748

journal_volume

212

pub_type

杂志文章

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