作者: Naoki Ichikawa , Chikae Ogura
关键词: ATPase 、 Bioorganic chemistry 、 Peptide sequence 、 Escherichia coli 、 Saccharomyces cerevisiae 、 ATP synthase 、 Biochemistry 、 Molecular biology 、 Yeast 、 Mitochondrion 、 Biology
摘要: Mitochondrial ATP synthase (F1F0-ATPase) is regulated by an intrinsic ATPase inhibitor protein. In this study, we overexpressed and purified human bovine inhibitors their properties were compared with those of a yeast inhibitor. The inhibited in similar way. also F1F0-ATPase, although the activity was about three times lower than mammalian inhibitors. All F1F0-ATPase activities all decreased at higher pH, but magnitude decrease different for each combination ATPase. results obtained study show that inhibitory mechanism basically shared mammals, require unique residues, which are lacking inhibitor, maximum activity. Common sites suggested.