DETERMINATION OF THE NUMBER OF DETERGENT MOLECULES ASSOCIATED WITH THE REACTION-CENTER PROTEIN ISOLATED FROM THE PHOTOSYNTHETIC BACTERIUM RHODOPSEUDOMONAS-VIRIDIS - EFFECTS OF THE AMPHIPHILIC MOLECULE 1,2,3-HEPTANETRIOL

被引:34
作者
GAST, P
HEMELRIJK, P
HOFF, AJ
机构
[1] Department of Biophysics, Huygens Laboratory, 2300 RA Leiden
关键词
PHOTOSYNTHESIS; MEMBRANE PROTEIN; DETERGENT; HEPTANETRIOL; BIO-BEADS;
D O I
10.1016/0014-5793(94)80625-X
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
Detergent-free reaction center (RC) proteins from the photosynthetic bacterium Rhodopseudomonas viridis were obtained using Bio-Beads SM-2. With these RCs, the amount of detergent molecules associated with the protein was measured by determining the detergent concentration al which re-solubilization occurred as a function of the RC concentration. For N,N-dimethyl dodecylamine-N-oxide (LDAO), Triton X-100 and B-octylglucoside 260 +/- 30,105 +/- 10 and 360 +/- 100 detergent molecules were necessary to dissolve the protein, respectively. With this technique we have studied the effect of the amphiphilic molecule 1,2,3-heptanetriol, which is essential in the crystallization process of these RCs. Addition of 5% 1,2,3-heptanetriol reduces the value for LDAO to 120 +/- 20 LDAO/RC, supporting the notion that crystallization of the RCs is promoted by increasing the number of protein-protein contacts.
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页码:39 / 42
页数:4
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