Abstract
Na+/K+-ATPase can hydrolyze some phosphatase substrates such as acetyl phosphate (AcP), p-nitrophenylphosphate (pNPP), and carbamylphosphate (CarbP) in the presence of Mg2+ and K+. When K+ is replaced with Na+, AcP is known to induce conformational changes and accumulate E1P and E2P in the presence of 2 M and 16 mM Na+, respectively (1,5,7,8). It was shown that some nucleotides and K+-phosphatase substrates can support some transport reactions (3). However there seems to be little evidence that pNPP or other phosphatase substrates induce conformational change and/or accumulate phosphoenzymes. To investigate this, the enzyme treated with N-(p-(2benzimidazolyl)phenyl)maleimide (BIPM) (6) or fluoroscein 5’-isothiocyanate (FITC) (48) were used to follow conformational changes. To measure the amount of phosphoenzyme, [32p]pNPP was synthesized.
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References
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© 1994 Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt
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Yamazaki, A., Kaya, S., Araki, Y., Shimada, A., Taniguchi, K. (1994). Phosphorylation of Na+/K+-ATPase by p-Nitrophenylphosphate and Other Phosphatase Substrates. In: Bamberg, E., Schoner, W. (eds) The Sodium Pump. Steinkopff. https://doi.org/10.1007/978-3-642-72511-1_117
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DOI: https://doi.org/10.1007/978-3-642-72511-1_117
Publisher Name: Steinkopff
Print ISBN: 978-3-642-72513-5
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