Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H(4)-H(5) loop of Na/K-ATPase

0142461 - FGU-C 20030066 RIV US eng J - Článek v odborném periodiku
Kubala, Martin - Plášek, J. - Amler, Evžen
Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H(4)-H(5) loop of Na/K-ATPase.
European Biophysics Journal With Biophysics Letters. Roč. 32, č. 4 (2003), s. 363-369. ISSN 0175-7571. E-ISSN 1432-1017
Výzkumný záměr: CEZ:AV0Z5011922; CEZ:MSM 113200001
Klíčová slova: TNP-ATP * scatchard plot * sudium pump
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 1.769, rok: 2003

We derived an explicit formula that makes it possible to estimate the dissociation constant for the binding of fluorescence probe to the enzyme. A series of computer simulation demonstrated clearly the advantage of non-linear regression using the explicit formula over the common linear regression using the Scatchard plot. Evaluation of TNP-ATP binding to the part of the large cytoplasmic loop of Na(+)/K(+)-ATPase verified this conclusion.
Trvalý link: http://hdl.handle.net/11104/0040164