Abstract
A detailed chemical and molecular mechanism by which the hydrolysis of ATP is coupled to the uphill movement of ions remains to be elucidated, even though a variety of studies have provided a wealth of information about structural and kinetic aspects of P-type pump mechanisms. Identification of the amino acid residues of the ATP site would provide important information for determining this chemical mechanism. Many results are consistent with the idea that fluorescein-5-isothiocyanate (FITC) labels a lysine that is part of the ATP site of the Na+/K+-, H+/K+-, sarcoplasmic reticulum (SR) Ca2+-, and plasma membrane (PM) Ca2+-pumps.
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© 1994 Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt
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Gatto, C., Milanick, M.A. (1994). Does Eosin Treat all P-type ATPases Equally?. In: Bamberg, E., Schoner, W. (eds) The Sodium Pump. Steinkopff. https://doi.org/10.1007/978-3-642-72511-1_108
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DOI: https://doi.org/10.1007/978-3-642-72511-1_108
Publisher Name: Steinkopff
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