ISOLATION AND CHARACTERIZATION OF A NEU PROTEIN-SPECIFIC ACTIVATING FACTOR FROM HUMAN ATL-2 CELL CONDITIONED MEDIUM

被引：18

作者：

DAVIS, JG

HAMURO, J

SHIM, CY

SAMANTA, A

GREENE, MI

DOBASHI, K

机构：

[1] UNIV PENN,SCH MED,DEPT PATHOL & LAB MED,DIV IMMUNOL,PHILADELPHIA,PA 19104

[2] UNIV PENN,SCH MED,DEPT PATHOL & LAB MED,CTR RECEPTOR BIOL,PHILADELPHIA,PA 19104

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 179卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)91747-Z

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：

The rat neu gene product is a 185 kD membrane bound tyrosine kinase that is closely related to, yet distinct from the epidermal growth factor receptor. The biochemical and cellular effects of a neu protein-specific activating factor (NAF) detected in human ATL-2 cell conditioned medium were recently described (1). To further characterize NAF, some of its physicochemical properties were examined and a method for purifying this factor from ATL-2 cell conditioned medium was developed. In these studies NAF was found to be heat stable and sensitive to the protease chymotrypsin. In addition, a method for purifying this activity was developed using a quantifiable, in vitro autophosphorylation assay system to measure NAF activity in fractions following ion-exchange and then reverse-phase HPLC. © 1991.

引用

页码：1536 / 1542

页数：7

共 10 条

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