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Selective extraction of 22 kDa and 10 kDa polypeptides from Photosystem II without removal of 23 kDa and 17 kDa extrinsic proteins
Authors:Ranjit K Mishra  Demetrios F Ghanotakis
Institution:(1) Department of Chemistry, University of Crete, Iraklion, Crete, Greece;(2) Institute of Molecular Biology and Biotechnology, F.O.R.T.H., Iraklion, Crete, Greece;(3) Department of Chemistry, University of Crete, P.O. Box 1470, 71 409 Iraklion, Crete, Greece
Abstract:Selective solubilization of Photosystem II membranes with the non-ionic detergent octyl thioglucopyranoside has allowed the isolation of a PS II system which has been depleted of the 22 and 10 kDa polypeptides but retains all three extrinsic proteins (33, 23 and 17 kDa). The PS II membranes which have been depleted of the 22 and 10 kDa species show high rates of oxygen evolution activity, external calcium is not required for activity and the manganese complex is not destroyed by exogenous reductants. When we compared this system to control PS II membranes, we observed a minor modification of the reducing side, and a conversion of the high-potential to the low-potential form of cytochrome b 559.Abbreviations Chl- chlorophyll - DCBQ- 2,5-dichloro-p-benzoquinone - DCMU- 3-(3,4-dichlorophenyl)-1,1-dimethylurea - ESR- electron spin resonance - MES- 2-(N-morpholino)ethanesulfonic acid - OTG- octyl-beta-d-thioglucopyranoside - PS II- Photosystem II - PEG- polyethylene glycol, Mr=6000 - Tris- 2-amino-2-hydroxyethylpropane-1,3-diol
Keywords:Photosystem II  oxygen evolution  extrinsic proteins  22 kDa polypeptide  10 kDa polypeptide
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