BIOLUMINESCENCE OF THE CA2+-BINDING PHOTOPROTEIN, AEQUORIN, AFTER HISTIDINE MODIFICATION
BIOLUMINESCENCE OF THE CA2+-BINDING PHOTOPROTEIN, AEQUORIN, AFTER HISTIDINE MODIFICATION
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DOI：
10.1016/0014-5793(93)80600-y
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发表时间：
1993-04-12
期刊：
影响因子：
3.5
通讯作者：
TSUJI, FI
中科院分区：
文献类型：
--
作者：
OHMIYA, Y;TSUJI, FI
采用定点诱变和焦碳酸二乙酯对水母发光蛋白中的 5 个组氨酸残基进行的修饰研究表明，His169 可能是水母发光蛋白中分子氧的结合位点。该残基的修饰导致活性完全丧失，而其余 4 个组氨酸残基的修饰产生了具有不同生物发光活性的突变水母发光蛋白。
Modification studies of the 5 histidine residues in aequorin employing site-directed mutagenesis and diethyl pyrocarbonate suggested that His169 may be the site of binding of molecular oxygen in aequorin. The modification of this residue led to complete loss of activity, whereas modification of the remaining 4 histidine residues yielded mutant aequorins with varying bioluminescence activities.