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光下D1/D2/Cytb559复合物中氨基酸残基的破坏和多肽的降解

LIGHT-INDUCED DAMAGE OF AMINO ACID RESIDUES AND DEGRADATION OF POLYPEPTIDES IN D1/D2/CYTOCHROME B559 COMPLEX

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【作者】 于振宝匡廷云卢荣禾唐崇钦汤佩松

【Author】 Yu Zhen bao, Kuang Ting yun, Lu Rong he, Tang Chong qin and Tang Pei song (Institute of Botany, Academia Sinica, Beijing 100044)

【机构】 中国科学院植物研究所!北京100044

【摘要】 光系统Ⅱ反应中心D1/D2/Cyt b559 复合物对光照十分敏感。不仅色素分子,而且多肽链上的氨基酸残基(如组氨酸和甲硫氨酸)均会受到破坏。光照同时引起D1 和D2 蛋白的降解。在SDS聚丙烯酰胺多肽电泳图谱上,D1/D2 二聚体的含量增多,同时有一条分子量大约为41 kD的新带出现。在光照后的暗放置过程中,氨基酸组成不再变化,但D1 和D2 蛋白的降解及大分子量片段的产生仍继续进行。对组氨酸和甲硫氨酸的破坏与D1、D2 蛋白的降解关系进行了初步的分析,推测在光破坏过程中,D1 和D2 蛋白也许发生了化学断裂和共价交联作用

【Abstract】 Photosystem Ⅱ reaction center D1/D2/Cyt b559 complex is very sensitive to light. Besides pigments, some amino acids, like histidine and methionine residues on the polypeptide chain, were damaged and D1 and D2 proteins were degraded by illumination. SDS PAGE analysis demonstrated an increased content of the D1 and D2 protein dimers and a new band with molecular weight of 41 kD after light treatment. Meanwhile, the D1 and D2 bands were shifted to apparent positions of higher molecular weight. During the consequent incubation in the dark following illumination, although there was no change in the composition of amino acids, the degradation process of D1 and D2 proteins and the production of 41 kD fragment continued. It was proposed that degradation of D1 and D2 proteins was probably due to the photodamage of some amino acids via chemical splitting and co valent cross linkage in this process.

【基金】 国家自然科学基金
  • 【文献出处】 植物学报 ,Acta Botanica Sinica , 编辑部邮箱 ,1995年04期
  • 【分类号】Q945.11
  • 【被引频次】12
  • 【下载频次】91
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