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
收藏
页码：255 / 259
页数：5
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