Image analysis of electron micrographs of ATPase (Coupling Factor TF1) from thermophilic bacteria and luminal epithelium of mouse urinary bladder.
Electron micrographs of two dimensional array of H+-ATPase (Coupling Factor TF1 from the thermophilic bacteria) and luminal epithelial protein of urinary bladder were obtained using negative staining method and freeze-fracture method, respectively. Images which showed good optical diffraction pattern were digitized by a computer-linked flat-bed two dimensional microdensitometer and processed digitally. The results of translational computer noise filtering showed that the outline of TF1 molecules looks like a hexagon or an asterisk in the presence of sodium azide which is a specific inhibitor of TF1 or AMPPNP which is an unsplitable analogue of ATP, respectively. The luminal epithelial protein also looks like a hexagon. Rotational harmonic analysis was carried out to examine the rotational symmetry of the filtered images of TF1. It was found that 2-fold or 6-fold symmetry is dominant in the presence of sodium azide or AMPPNP, respectively.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology; D000818:Animals; D001386:Azides / Q000494:pharmacology; D001419:Bacteria / Q000201:enzymology*; D004848:Epithelium / Q000201:enzymology; D006358:Hot Temperature; D051379:Mice; D008854:Microscopy, Electron; D011487:Protein Conformation; D006180:Proton-Translocating ATPases; D013045:Species Specificity; D001743:Urinary Bladder / Q000201:enzymology*
D001386:Azides; D000266:Adenylyl Imidodiphosphate; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases