摘要
研究了羧基修饰剂DCCD对泛醌结合蛋白QPs重组活力的影响;用0.1%TritonX-100增溶QPs后,用250mol/molQPs的DCCD于室温处理5min,处理后的QPs丧失约50%与琥珀酸脱氢酶的重组活力。先将QPs与琥珀酸脱氢酶重组再用DCCD处理没有发现重组的琥珀酸泛醌还原酶活性的降低。此结果说明QPs中存在重组活性必需的羧基。
QPs was named as the Q-binding protein in succinate-Q reductase. It was isolated in 1980 by several laboratories. QPs can be reconstituted with succinate dehydrogenase (SDH) to become the reconstitutively active succinate-Q reductase. Some amino groups in succinate dehydrogenase was found to be necessary for the activity of reconstitution.This result implicated that in QPs there must be some negative charged groups which were necessary for the reconstitution.DCCD was used to modify the carboxyl groups of QPs,and proved that some carboxyl groups were responsible for the reconstitutive activity.
关键词
泛醌结合蛋白
化学修饰
羧基
重组活性
Q-binding protein, Chemical modification, Succinate-Q reductase