TIME-RESOLVED INTRINSIC FLUORESCENCE OF ENZYME-I - THE MONOMER DIMER TRANSITION

被引：9

作者：

CHAUVIN, F

TOPTYGIN, D

ROSEMAN, S

BRAND, L

机构：

[1] JOHNS HOPKINS UNIV,DEPT BIOL,BALTIMORE,MD 21218

[2] JOHNS HOPKINS UNIV,MCCOLLUM PRATT INST,BALTIMORE,MD 21218

来源：

BIOPHYSICAL CHEMISTRY | 1992年 / 44卷 / 03期

关键词：

PHOSPHOTRANSFERASE SYSTEM ENZYME-I; TIME-RESOLVED FLUORESCENCE; MONOMER DIMER EQUILIBRIUM;

D O I：

10.1016/0301-4622(92)80049-B

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：

Enzyme I of the bacterial phosphotransferase system can exist in a monomer/dimer equilibrium which may have functional significance. Each monomer contains two tryptophan residues. It is demonstrated that the decay of both the monomer and the dimer can be described by a biexponential. The decay times depend on the temperature and at 6-degrees-C the decay times are tau1 = 0.4 ns and tau2 = 3.2 ns for the monomer and tau3 = 3.2 ns and tau4 = 7.2 ns for the dimer form of the enzyme. The changes in the fluorescence decay parameters can be utilized to measure the equilibrium constant for the monomer/dimer transition.

引用

页码：163 / 173

页数：11

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