HUMAN TOPOISOMERASE-I IS PHOSPHORYLATED IN-VITRO ON ITS AMINO-TERMINAL DOMAIN BY PROTEIN-KINASE NII

被引：13

作者：

CARDELLINI, E

BRAMUCCI, M

GIANFRANCESCHI, GL

DURBAN, E

机构：

[1] UNIV CAMERINO, DIPARTIMENTO BIOL MCA, I-62032 CAMERINO, ITALY

[2] BAYLOR COLL MED, DEPT PHARMACOL, HOUSTON, TX 77030 USA

来源：

BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1994年 / 375卷 / 04期

关键词：

PHOSPHORYLATION SITES; PROTEIN KINASE NII; TOPOISOMERASE I;

D O I：

10.1515/bchm3.1994.375.4.255

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Topoisomerase I purified from HeLa cells was phosphorylated in vitro with protein kinase NII (pkNII) purified from calf thymus: this phosphorylation was inhibited by heparin. A peptide containing a sequence corresponding to a putative pkNII phosphorylation site in topoisomerase I was synthesized and phosphorylated with pkNII. HPLC and two-dimensional analysis show identity between the synthetic phosphorylated peptide and one topoisomerase phosphopeptide indicating Ser(10) as one of the in vitro pkNII phosphorylation sites in topoisomerase I.

引用

页码：255 / 259

页数：5

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