Mechanism of K+ interaction with fluorescein 5'-isothiocyanate-modified Na+,K(+)-ATPase
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منابع مشابه
Stoichiometry of phosphorylation to fluorescein 5-isothiocyanate binding in the Ca2+-ATPase of sarcoplasmic reticulum vesicles.
In an attempt to establish the stoichiometry of phosphorylation in the Ca2+-ATPase of sarcoplasmic reticulum (SR) vesicles, phosphorylation by ATP (or Pi) or labeling by fluorescein 5-isothiocyanate (FITC) was performed with the SR vesicles under the conditions in which almost all the phosphorylation sites or FITC binding sites are phosphorylated or labeled. The resulting vesicles were solubili...
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Several model compounds containing thiol and/or amino groups (mercaptoethanol, glutathione, cysteine, ethanolamine, glycine) were studied with respect to their reactivity towards fluorescein isothiocyanate (followed spectrophotometrically at 504 and 412 nm), stability of product and long-wave absorption maximum of the fluorescein residue attached. Thiol groups reacted by far more readily than a...
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Unlike skeletal muscle sarcoplasmic reticulum, canine cardiac sarcoplasmic reticulum hydrolyzes GTP in ways that are similar and different from ATP hydrolysis. Also, ATP and ATP analogues inhibit GTPase activity noncompetitively with a Ki compatible with the high affinity ATP-binding site (c.f. Tate, C.A., Bick, R.J., Blaylock, S., Youker, K., Scherer, N.M., and Entman, M.L. (1989) J. Biol. Che...
متن کاملThe fluorescein isothiocyanate-binding site of the plasma-membrane H+-ATPase of Neurospora crassa.
The mammalian (Na+,K+), Ca2+-, and (H+,K+)-ATPases contain a well-characterized lysine residue that reacts with fluorescein 5'-isothiocyanate (FITC); enzymatic activity is protected by ATP, suggesting that the residue is located in or near the nucleotide-binding domain. In this study, the plasma-membrane H+-ATPase of Neurospora crassa is also shown to be sensitive to FITC. The reaction occurs w...
متن کاملCompetition between decavanadate and fluorescein isothiocyanate on the Ca2+-ATPase of sarcoplasmic reticulum.
The binding of vanadate and fluorescein isothiocyanate to the Ca2+-transport ATPase of sarcoplasmic reticulum (EC 3.6.1.3) was analyzed. Monovanadate binds to the Ca2+-transport ATPase at a single high affinity site (site 1), that is presumably related to the binding site for inorganic orthophosphate, and to one of the two sites for decavanadate. Binding of vanadate to this site stabilizes the ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85397-8