Solubilization and partial purification of a thylakoidal enzyme of spinach involved in the processing of D1 protein

FEBS Letters

Inagaki, N.¹  Satoh, K.¹  Fujita, S.¹ 

[1] Department of Biology, Faculty of Science, Okayama University, Okayama 700, Japan

关键词: Protein;    D1;    Photosystem II;    Protease;    processing;    SDS-PAGE;    (Spinach thylakoid);    Chl;    chlorophyll;    PS;    photosystem;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(89)80286-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The enzyme involved in the processing of D1 precursor protein was solubilized from spinach thylakoids by Triton X-100 treatment and then partially purified in the presence of the detergent by Sephadex G-75 gel-filtration chromatography. The apparent molecular mass of the enzyme was estimated via this procedure to be about 34 kDa. The D1 precursor protein translated from the extracted spinach chloroplast RNA by a wheat germ cell-free system was used here as a substrate in measurements of the activity.

【 授权许可】

Unknown