ISOLATION OF MITOTIC P34CDC2 APOENZYME FROM HUMAN-CELLS

被引：5

作者：

MEIKRANTZ, W ^{[1
]}

FELDMAN, RP ^{[1
]}

SLADICKA, MM ^{[1
]}

HO, D ^{[1
]}

KRUPNICK, J ^{[1
]}

ANDERSON, K ^{[1
]}

SCHLEGEL, RA ^{[1
]}

机构：

[1] PENN STATE UNIV,DEPT MOLEC & CELL BIOL,UNIVERSITY PK,PA 16802

来源：

FEBS LETTERS | 1991年 / 291卷 / 02期

关键词：

MITOSIS; PHOSPHOTYROSINE; P34CDC2; HUMAN;

D O I：

10.1016/0014-5793(91)81281-C

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：

A simple procedure was devised for isolating from homogenates of mitotic cells the human homolog to the fission yeast cdc2 gene product. The identity of the purified protein was established with anti-p34cdc2 antibodies and p13sucl, both specific ligands for p34cdc2. Active-site labeling with oxidized [alpha-P-32]ATP showed the purified molecule to be an ATP-binding protein. Its ability to phosphorylate casein but not histone, and its phosphorylation on tyrosine, detected by anti-phosphotyrosine antibodies, indicates the form of p34cdc2 purified is the inactive or apoenzyme form. Purified quantities of human p34cdc2 should be of considerable value in establishing the mechanism of its activation at mitosis by phosphatases.

引用

页码：192 / 194

页数：3

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