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

页码：187 / 189

页数：3

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