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Solubilization and partial purification of a thylakoidal enzyme of spinach involved in the processing of D1 protein
Author(s) -
Inagaki N.,
Fujita S.,
Satoh K.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80286-8
Subject(s) - spinach , sephadex , size exclusion chromatography , enzyme , thylakoid , solubilization , biochemistry , chromatography , substrate (aquarium) , chloroplast , molecular mass , chemistry , biology , ecology , gene
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.