2’(3’)-0-[N- [2- [3- [5-fluoresceinyl] thioureido] ethyl] carbamoyl] adenosine 5’-triphosphate and its Cr(H20)4 and Co(NH3)4 Complex Derivatives are New Fluorescent Tools for Labelling ATP Binding Sites of Na+/K+-ATPase

Title:

2’(3’)-0-[N- [2- [3- [5-fluoresceinyl] thioureido] ethyl] carbamoyl] adenosine 5’-triphosphate and its Cr(H20)4 and Co(NH3)4 Complex Derivatives are New Fluorescent Tools for Labelling ATP Binding Sites of Na+/K+-ATPase

Creator:

Linnertz, H., Lastres Becker, I., Krumscheid, R., Amler, E., Thoenges, D., and Schoner, W.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:15d88dc0-b93b-47eb-8b6c-80703054d2d0
uuid:15d88dc0-b93b-47eb-8b6c-80703054d2d0

Subject:

Na + /K+-ATPase, complex derivatives of ATP, low-affinity ATP-binding site, and high-affinity ATP binding site

Type:

article, model:article, and TEXT

Description:

2’(3’)-0-[N- [2- [3- [5-fluoresceinyl] thioureido] ethyl] carbamoyl] adenosine 5’-triphosphate (FEDA-ATP), a spectroscopic tool used for studying skeletal muscle myosin ATPase subfragment 1, was applied to Na+/K+- ATPase (EC 3.6.1.37). In contrast to the myosin subfragment, we found that FEDA-ATP is not a substrate for Na + /K + -ATPase. On the other hand, FEDA-ATP showed an affinity for both the low (E2, K<j = 2001MM) and the high (Ei, Kd = 22,«M) affinity ATP-binding sites. When the microscopic affinities of FEDA-ATP were used for calculating the macroscopic affinity in the overall reaction according to Kj = (KdEl*KdE2)1/2, the experimentally measured inhibition constant of 66,wM was obtained. To evoke irreversible binding inhibitors, FEDA-ATP was transferred in its chromium (III) and cobalt(III) complex analogs, which are suitable tools for labelling the ATP binding sites of Na + /K+ -ATPase in a specific way.

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 1997 Volume:46 | Number:5

Harvested from:

CDK

Metadata only:

false