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.
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页码：1536 / 1542
页数：7
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