GLYCINEBETAINE STABILIZES THE ASSOCIATION OF EXTRINSIC PROTEINS WITH THE PHOTOSYNTHETIC OXYGEN-EVOLVING COMPLEX

被引：147
|
作者：
MURATA, N [1 ]
MOHANTY, PS [1 ]
HAYASHI, H [1 ]
PAPAGEORGIOU, GC [1 ]
机构：
[1] GRAD UNIV ADV STUDIES,DEPT MOLEC BIOMECH,OKAZAKI 444,JAPAN
来源：
FEBS LETTERS | 1992年 / 296卷 / 02期
关键词：
GLYCINEBETAINE; OXYGEN EVOLUTION; PHOTOSYNTHESIS; PHOTOSYSTEM; 2; COMPLEX; SALT EFFECT;
D O I：
10.1016/0014-5793(92)80376-R
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：
The photosynthetic oxygen-evolving activity of the photosystem 2 complex, prepared from spinach, was labile when the complex was exposed to high-salt conditions under which the extrinsic proteins were dissociated from the complex. Glycinebetaine prevented the dissociation of the 18-kDa and the 23-kDa extrinsic proteins from the photosystem 2 complex in the presence of 1 M NaCl. It also prevented the dissociation of the 33-kDa extrinsic protein from the complex in the presence of 1 M MgCl2 or 1 M CaCl2. The oxygen-evolving activity of the photosystem 2 complex was stabilized by glycinebetaine when the complex was subjected to treatment with NaCl and MgCl2.
引用
收藏
页码：187 / 189
页数：3
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