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Correction published on 8 January 2009, see Sensors 2009, 9(1), 377.
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Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds

Vinča Institute of Nuclear Sciences, Department of Physical Chemistry, 11001 Belgrade, Republic of Serbia
Institute of Medicinal Chemistry, University School of Medicine, University of Belgrade, Višegradska 12, Belgrade, Republic of Serbia
Author to whom correspondence should be addressed.
Sensors 2008, 8(12), 8321-8360;
Received: 3 November 2008 / Revised: 9 November 2008 / Accepted: 11 December 2008 / Published: 15 December 2008
(This article belongs to the Special Issue Toxin Sensors)
This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na+,K+-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na+,K+-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na+,K+-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research. View Full-Text
Keywords: Na+; K+-ATPase; toxic agents; inhibition; detection; sensor Na+; K+-ATPase; toxic agents; inhibition; detection; sensor
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MDPI and ACS Style

Vasić, V.; Momić, T.; Petković, M.; Krstić, D. Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. Sensors 2008, 8, 8321-8360.

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