BINDING SHIFT ASSAY OF PARVALBUMIN, CALMODULIN AND CARBONIC-ANHYDRASE BY HIGH-PERFORMANCE CAPILLARY ELECTROPHORESIS

被引:33
作者
KAJIWARA, H
HIRANO, H
OONO, K
机构
[1] National Institute of Agrobiological Resources, Tsukuba, Ibaraki
来源
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS | 1991年 / 22卷 / 04期
关键词
CALMODULIN; CAPILLARY ELECTROPHORESIS; CE; HIGH-PERFORMANCE CAPILLARY ELECTROPHORESIS; HPCE; CARBONIC ANHYDRASE; PARVALBUMIN;
D O I
10.1016/0165-022X(91)90032-R
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Shifts in mobility caused by binding of Ca2+ to calmodulin and parvalbumin were studied using high-performance capillary electrophoresis in a Tris-glycine buffer, rather than conventional polyacrylamide gel electrophoresis which requires larger amounts of sample and longer assay time. A Zn2+-binding protein, carbonic anhydrase, also showed a partial shift in mobility following Zn2+-binding.
引用
收藏
页码:263 / 268
页数:6
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