Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds
Apstrakt
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.
Ključne reči:
Na+,K+-ATPase / toxic agents / inhibition / detection / sensorIzvor:
Sensors, 2008, 8, 12, 8321-8360Finansiranje / projekti:
- Istraživanje mehanizma interakcija biološki aktivnih jedinjenja sa biomolekulima (RS-MESTD-MPN2006-2010-142051)
Napomena:
- Correction: https://vinar.vin.bg.ac.rs/handle/123456789/3626
DOI: 10.3390/s8128321
ISSN: 1424-8220
PubMed: 27873990
WoS: 000261948200046
Scopus: 2-s2.0-58149197790
Institucija/grupa
VinčaTY - JOUR AU - Vasić, Vesna M. AU - Momić, Tatjana AU - Petković, Marijana AU - Krstić, Danijela Z. PY - 2008 UR - https://vinar.vin.bg.ac.rs/handle/123456789/3598 AB - 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. T2 - Sensors T1 - Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds VL - 8 IS - 12 SP - 8321 EP - 8360 DO - 10.3390/s8128321 ER -
@article{ author = "Vasić, Vesna M. and Momić, Tatjana and Petković, Marijana and Krstić, Danijela Z.", year = "2008", abstract = "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.", journal = "Sensors", title = "Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds", volume = "8", number = "12", pages = "8321-8360", doi = "10.3390/s8128321" }
Vasić, V. M., Momić, T., Petković, M.,& Krstić, D. Z.. (2008). Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. in Sensors, 8(12), 8321-8360. https://doi.org/10.3390/s8128321
Vasić VM, Momić T, Petković M, Krstić DZ. Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. in Sensors. 2008;8(12):8321-8360. doi:10.3390/s8128321 .
Vasić, Vesna M., Momić, Tatjana, Petković, Marijana, Krstić, Danijela Z., "Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds" in Sensors, 8, no. 12 (2008):8321-8360, https://doi.org/10.3390/s8128321 . .