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THE REDUCTION OF FERRYL MYOGLOBIN BY ERGOTHIONEINE - A NOVEL FUNCTION FOR ERGOTHIONEINE
被引:74
|
作者
:
ARDUINI, A
论文数:
0
引用数:
0
h-index:
0
机构:
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
ARDUINI, A
[
1
]
EDDY, L
论文数:
0
引用数:
0
h-index:
0
机构:
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
EDDY, L
[
1
]
HOCHSTEIN, P
论文数:
0
引用数:
0
h-index:
0
机构:
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
HOCHSTEIN, P
[
1
]
机构
:
[1]
UNIV SO CALIF,INST TOXICOL,LOS ANGELES,CA 90033
来源
:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
|
1990年
/ 281卷
/ 01期
关键词
:
D O I
:
10.1016/0003-9861(90)90410-Z
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
:
In this paper, we demonstrate that ergothioneine (ES), a naturally occurring thiolhistidine, reduces ferrylmyoglobin (MbIV) to MbIII when the former (ferryl species) is produced by exposing either deoxy MbII or MbIII to H2O2. The reduction of MbIV to MbIII by ES yields the disulflde of ES which the addition of GSH promptly reduces back to ES. The addition of ES (100 μm) in the perfusion buffer of Langendorff rat heart preparations exposed to a brief period of ischemia prevents the myocardial damage (lactate dehydrogenase release) which accompanies reperfusion. The results of these experiments support a view that ES and its redox couple GSH might function in a Mb redox cycle. © 1990.
引用
收藏
页码:41 / 43
页数:3
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