第24卷第3期
2012年3月
化学研究与应用
Chemical Research and Application
,
Mar.,2012
文章编号:(2012)03-0370-05
金属离子Zn2+对精氨酸酶抑制作用的研究
史竞艳h,王志勇2,刘欲文2,汪存信2
(,湖北武汉430415;
,湖北武汉43072)
摘要:在37。C,pH=,40 mmol・L“的巴比妥钠一盐酸缓冲体系中,利用微量热法研究了金属离子zn“对牛
肝精氨酸酶催化L一精氨酸水解反应的影响。实验表明,zn“对精氨酸酶催化反应存在着明显抑制作用,其抑
制类型为竞争性可逆抑制,
10~tool・L~。根据其抑制类型和离子半径,推测
Zn2+对精氨酸酶的抑制主要是夺取Mn“的位置,从而使酶失活。
关键词:精氨酸酶;锌;竞争性可逆抑制;微量热法
中图分类号:
文献标识码:A
Investigation
on
the inhibition against arginase catalyzed reaction by Zn2+
SHI
Jing—yanl’,WANG
,LIU ,WANG Cun—xin2
(
of Chemistry and Environment Engineering,Wuhan Bioengineering Institute,Wuhan 430415,China
of Chemistry and Molecular Sciences,Wuhan University,Wuhan
430072,China)
Abstract:The influence of Zn2+on
arginase
catalyzed reaction was studied by mierocalorimetry at 37℃,pH=,40 mmol・L一1
sodium acid buffer result indicated that Zn2+has remarkable inhibition effect
the catalytic
activity of
arginase
and the inhibitory type belongs
the petitive inhibition with the inhibition constants ×10—7
mol・L~.According
the inhibition type and ion radius,we suggest that the for
inhibition
is
petition of Zn2+on the
active site
of
arginase
and thus
inhibits
the reaction
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