Ca2+-ATPase from chicken (Gallus domesticus) erythrocyte plasma membrane: effects of calmodulin and taurine on the Ca2+-dependent ATPase activity and Ca2+ uptake

Alves-Ferreira, Marcelo; Scofano, Helena M.; Ferreira‐Pereira, Antônio

doi:10.1016/s0305-0491(99)00008-5

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Electrophoresis and Western Blot Analysis1

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2022

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Cited by 6 publications

(1 citation statement)

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“…Nucleated erythrocyte ghosts were extracted in accordance with the methods of (Alves- Ferreira et al, 1999). Ghosts were separated by SDS-PAGE (5-10% acrylamide density gradient electrophoresis).…”

Section: Electrophoresis and Western Blot Analysismentioning

confidence: 99%

Alteration Young’s moduli by protein 4.1 phosphorylation play a potential role in the deformability development of vertebrate erythrocytes

Tang

Lei

Xiong

et al. 2014

Journal of Biomechanics

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Section: Electrophoresis and Western Blot Analysismentioning

confidence: 99%

Alteration Young’s moduli by protein 4.1 phosphorylation play a potential role in the deformability development of vertebrate erythrocytes

Tang

Lei

Xiong

et al. 2014

Journal of Biomechanics

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Blood

Scanes

2022

Sturkie's Avian Physiology

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3-O-Methylfluorescein phosphate as a fluorescent substrate for plasma membrane Ca2+-ATPase

Freire

Mignaco

Carvalho-Alves

et al. 2002

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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3-O-methylfluorescein phosphate hydrolysis, catalyzed by purified erythrocyte Ca2+-ATPase in the absence of Ca2+, was slow in the basal state, activated by phosphatidylserine and controlled proteolysis, but not by calmodulin. p-Nitrophenyl phosphate competitively inhibits hydrolysis in the absence of Ca2+, while ATP inhibits it with a complex kinetics showing a high and a low affinity site for ATP. Labeling with fluorescein isothiocyanate impairs the high affinity binding of ATP, but does not appreciably modify the binding of any of the pseudosubstrates. In the presence of calmodulin, an increase in the Ca2+ concentration produces a bell-shaped curve with a maximum at 50 microM Ca2+. At optimal Ca2+ concentration, hydrolysis of 3-O-methylfluorescein phosphate proceeds in the presence of fluorescein isothiocyanate, is competitively inhibited by p-nitrophenyl phosphate and, in contrast to the result observed in the absence of Ca2+, it is activated by calmodulin. In marked contrast with other pseudosubstrates, hydrolysis of 3-O-methylfluorescein phosphate supports Ca2+ transport. This highly specific activity can be used as a continuous fluorescent marker or as a tool to evaluate partial steps from the reaction cycle of plasma membrane Ca2+-ATPases.

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Ca2+-ATPase from chicken (Gallus domesticus) erythrocyte plasma membrane: effects of calmodulin and taurine on the Ca2+-dependent ATPase activity and Ca2+ uptake

Cited by 6 publications

References 45 publications

Alteration Young’s moduli by protein 4.1 phosphorylation play a potential role in the deformability development of vertebrate erythrocytes

Alteration Young’s moduli by protein 4.1 phosphorylation play a potential role in the deformability development of vertebrate erythrocytes

Blood

3-O-Methylfluorescein phosphate as a fluorescent substrate for plasma membrane Ca2+-ATPase

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