INTERACTION OF THE CATALYTIC SUBUNITS OF PROTEIN PHOSPHATASE-1 AND PHOSPHATASE-2A WITH INHIBITOR-1 AND INHIBITOR-2 - A FLUORESCENT STUDY WITH SULFHYDRYL-SPECIFIC PYRENE MALEIMIDE

被引:6
作者
CSORTOS, C [1 ]
MATKO, J [1 ]
ERDODI, F [1 ]
GERGELY, P [1 ]
机构
[1] DEBRECEN UNIV MED,SCH MED,DEPT BIOPHYS,H-4012 DEBRECEN,HUNGARY
基金
匈牙利科学研究基金会;
关键词
D O I
10.1016/0006-291X(90)90367-V
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 catalytic subunits of protein phosphatase-1 and 2A were covalently modified in their reactive sulfhydryl groups with N-(3-Pyrene) maleimide resulting in fluorescent labeling of the proteins to an extent of 0.85 and 0.9 mole dye/mole enzyme, respectively. The reaction of the sulfhydryl group led to the partial inactivation of both phosphatase-1 and 2A. Inhibitor-1 and inhibitor-2 increased markedly the fluorescence intensity of the dye-phosphatase-1 conjugate implying that the labeled enzyme retained its ability to bind these proteins. In contrast, inhibitor-1 or inhibitor-2 had no influence on the fluorescence of the dye-phosphatase-2A conjugate. No change in either the fluorescence intensity or polarization of labeled phosphatase-1 and 2A was observed in the presence of thiophosphorylase a, suggesting a lack of interaction of these enzyme forms with the substrate after modification of the reactive sulfhydryl group. © 1990.
引用
收藏
页码:559 / 564
页数:6
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