High impact information on Anthroylouabain

• The energy transfer seen upon AO binding to Na+,K+-ATPase suggests the presence of one completely quenched or two highly quenched enzyme Trp residues approximately 10 and approximately 17 A, respectively, from the anthroyl moiety [1].
• This is consistent with the energy transfer seen upon AO binding to mAb 26-10 and suggests that Trp-H100, which is part of the antibody's cardiac glycoside binding site, is a major determinant of the fluorescence properties of bound AO [1].
• Labeling stoichiometries from 1 to 11 mol of lucifer yellow CH per mol of beta were obtained without inhibition of (Na,K)ATPase activity and without significant alteration of the anthroylouabain binding capacity or its association and dissociation kinetics [2].
• Exposure of opercular membranes from freshwater tilapia to 2 microM anthroylouabain did not result in significant staining [3].
• Because phosphorylation of (Na,K)-ATPase is necessary to bind anthroylouabain, only functional enzyme is detected by this method [4].

Biological context of Anthroylouabain

• These data suggest a model for the localization of the terminal moieties of the oligosaccharides that places them, on average, about 18 A from the AO binding site and this distance or less from the extracellular membrane surface [5].

Anatomical context of Anthroylouabain

• The yolk-sac MR cells were immunoreacted to the antibody (alpha5) against the alpha subunit of avian Na-K-ATPase and were double-labeled with anthroylouabain and dimethylaminostyrylethyl-pyridiniumiodine, suggesting the existence and activity of Na-K-ATPase in these cells [6].

Associations of Anthroylouabain with other chemical compounds

• In contrast, the generated model of AO complexed to Fab 40-50 [Jeffrey, P. D., et al. (1995) J. Mol. Biol. 248, 344] shows a heavy chain Tyr residue (Tyr-H100) which is part of the cardiac glycoside binding site, located approximately 10 A from the anthroyl moiety [1].

Gene context of Anthroylouabain

• Anthroylouabain staining was observed in both prolactin- and saline-injected fish, and no significant effect on Na+,K(+)-adenosinetriphosphatase activity was seen in either opercular membrane or gill tissue [7].

References