PROPERTIES OF A NOVEL NITRIC OXIDE-STIMULATED ADP-RIBOSYLTRANSFERASE

被引:58
作者
BRUNE, B [1 ]
LAPETINA, EG [1 ]
机构
[1] BURROUGHS WELLCOME CO,DIV CELL BIOL,RES TRIANGLE PK,NC 27709
关键词
D O I
10.1016/0003-9861(90)90493-I
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 novel ADP-ribosyltransferase is present in the cytosolic fraction of various cells. The kinetic behavior and physical properties of this enzyme's activity are clearly distinguished from other known cytosolic ADP-ribosyltransferases. Agents that release nitric oxide, such as sodium nitroprusside, greatly stimulated this activity, although this effect was dependent on the presence of intact thiol groups. Dithiothreitol, reduced glutathione, or cysteine was needed for activation of the enzyme, while N-ethylmaleimide inhibited enzyme activity. High concentrations of phosphate had a slight stimulatory effect, while high concentrations of sodium chloride and thiocyanate were inhibitory. ATP also inhibited this activity. This cytosolic ADP-ribosyltransferase is clearly distinguished from other known and characterized cytosolic transferases. Its activation by biologically active nitric oxide suggests an important role for this enzymatic activity. © 1990.
引用
收藏
页码:286 / 290
页数:5
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