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巯基修饰对中华仓鼠二氢叶酸还原酶的激活
15 1 Vol. 15, No . 1
1999 2 Chinese Journal of Biochemistry and Molecular Biology Feb. 1999
·研究简报·
范映辛 李震宇 周筠梅
( 中国科学院生物物理研究所, 生物大分子国家重点实验室, 北京 100101)
Activation of Dihydrofolate Reductase from Chinese Hamster
-
by Sulfhydryl modification
, ,
FAN Yingxin LI Zhenyu ZHOU Junmei
(N ational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese A cademy of Scinence, Beij ing 100101)
AbstractThe activity of dihydrofolate reductase from Chinese hamster can be increased 2. 4, 1. 8
and 1. 4 fold upon the modification of its sulfhydryl group w ith p -hydroxylmercuribenzoate (p -
) , - ( - ) 5, 5 - ( 2- )
HM B p hydroxylmercuriphenylsulfonate p HMPS and dithiobis nitrobenzoate acid
( ) . 400- -
DT NB respectively T he activation of the enzyme by fold molar excess of p HMB w as a
- 1
monophasic process with a rate constant of 0. 015 s . T he extents of activation as w ell as the rate
of activation w as low ered in the presence of the substrate dihydrofolate, but w as unaffected by the
.
other substrate of NADPH The modified enzyme could be further activated by guanidine hy-
drochloride and potassium chloride, but not by urea, w hich suggesting that the mechanism of the
activation of dihydrofolate reductase by ions w as different from that by protein denaturants and
- .
sulfhydryl modifyi
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