3,4-DICHLOROISOCOUMARIN, A SERINE PROTEASE INHIBITOR, INACTIVATES GLYCOGEN PHOSPHORYLASE-B

被引:16
作者
RUSBRIDGE, NM [1 ]
BEYNON, RJ [1 ]
机构
[1] UNIV LIVERPOOL,DEPT BIOCHEM,PROTEOLYSIS RES GRP,POB 147,LIVERPOOL L69 3BX,ENGLAND
关键词
3,4-Dichloroisocoumarin; Glycogen phosphorylase b;
D O I
10.1016/0014-5793(90)80991-Q
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
3,4-Dichloroisocoumarin (3,4-DCI) is a highly reactive, mechanism-based inhibitor of serine proteases. We show here that glycogen phosphorylase b is also inactivated by this inhibitor, in a mechanism that parallels the inactivation of serine proteases, but involving multiple sites of covalent modification. Such a process may compromise studies in which 3,4-DCI is used to arrest proteolysis of a second native protein which may itself be modified. © 1990.
引用
收藏
页码:133 / 136
页数:4
相关论文
共 6 条
[1]  
BEYNON RJ, 1985, COMPUT APPL BIOSCI, V1, P111
[2]   SEMICONTINUOUS ASSAY FOR GLYCOGEN-PHOSPHORYLASE [J].
CARNEY, IT ;
BEYNON, RJ ;
KAY, J ;
BIRKET, N .
ANALYTICAL BIOCHEMISTRY, 1978, 85 (01) :321-324
[3]   REACTION OF SERINE PROTEASES WITH SUBSTITUTED ISOCOUMARINS - DISCOVERY OF 3,4-DICHLOROISOCOUMARIN, A NEW GENERAL MECHANISM BASED SERINE PROTEASE INHIBITOR [J].
HARPER, JW ;
HEMMI, K ;
POWERS, JC .
BIOCHEMISTRY, 1985, 24 (08) :1831-1841
[4]   DETERMINATION OF INORGANIC PHOSPHATE IN PRESENCE OF LABILE ORGANIC PHOSPHATES [J].
PARVIN, R ;
SMITH, RA .
ANALYTICAL BIOCHEMISTRY, 1969, 27 (01) :65-&
[5]   MECHANISM-BASED ISOCOUMARIN INHIBITORS FOR SERINE PROTEASES - USE OF ACTIVE-SITE STRUCTURE AND SUBSTRATE-SPECIFICITY IN INHIBITOR DESIGN [J].
POWERS, JC ;
KAM, CM ;
NARASIMHAN, L ;
OLEKSYSZYN, J ;
HERNANDEZ, MA ;
UEDA, T .
JOURNAL OF CELLULAR BIOCHEMISTRY, 1989, 39 (01) :33-46
[6]  
PRICE NC, 1989, PROTEOLYTIC ENZYMES, P163