The role of Mg++-ATPase (actomyosin-like protein) in maintaining the biconcave shape of erythrocytes

Mircevová, L

doi:10.1007/bf00996145

Cited by 13 publications

(1 citation statement)

References 25 publications

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“…Quist and Roufogalis (32) established that this enzyme influences the viscosity of the blood. In our laboratory we found that Mg-ATPase (for mer additional denomination 'actomyosin-like protein') participated in maintaining the red cell shape (33). Very probably this enzyme also influences the passive K+ transport (34) and is associated with the permeation of phosphates, sugars and other substances across the mem brane (35).…”

Section: Discussionmentioning

confidence: 99%

Activation of Mg-ATPase (Spectrin-Dependent ATPase) by Ca^2+

Mircevová¹,

Kotva²,

Kodı́ček³

et al. 1979

Enzyme

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The dependence of saponin-stimulated Mg-ATPase activity in the erythrocyte membrane on Ca^2+ concentration was studied. In the membrane of freshly sampled human erythrocytes we found for this enzyme and Ca2+ an apparent dissociation constant of 0.611 µmol/l (SE ± 0.106 µmol/l) and Hill coefficient of 0.93 (SE ± 0.05). The enzyme is in most probability identical with Ca.Mg-ATPase of high affinity to Ca^2+ described also as spectrin-dependent Ca,Mg-ATPase.

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Section: Discussionmentioning

confidence: 99%

Activation of Mg-ATPase (Spectrin-Dependent ATPase) by Ca^2+

Mircevová¹,

Kotva²,

Kodı́ček³

et al. 1979

Enzyme

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Is there any connection between heat inactivation of spectrin‐dependent ATPase and loss of smooth biconcave shape of red cells?

Mircevová¹,

Kodı́ček²,

Marík³

1983

Cell Biochemistry & Function

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Spectrin-dependent ATPase activity was measured in membranes from native human erythrocytes and erythrocytes heated for 20 min at different temperatures. This activity was found to decline when the erythrocytes were heated at 48 degrees C and higher. The break in ATPase activity corresponds to morphological changes in erythrocytes found by Crome and Mollison [Brit. J. Haematol. (1964) 10, 137]. The role of spectrin-dependent ATPase in erythrocyte shape maintenance is discussed.

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Tellurite effect on ATPase activity of contractile membrane protein

Mircevová

Kodı́ček

1991

Cell Biochemistry & Function

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The effect of tellurite on ATPase activity of the contractile membrane protein in human erythrocytes was studied. Tellurite, even at a concentration of 0.01 mM, inhibited 25 per cent of the saponin-stimulated ATPase activity of the contractile membrane protein; the inhibition increased with increasing tellurite concentration, and was reversible. On the other hand, in erythrocytes preincubated with tellurite, the ATPase activity of the membrane contractile protein, non-stimulated by saponin, increased, and the increase was further enhanced by washing the erythrocytes. The behaviour is analogous to the tellurite effect on erythrocyte morphology: incubation of erythrocytes with tellurite caused morphological changes which were more pronounced after removing the tellurite by washing. The complex effect of tellurite is discussed.

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The role of Mg++-ATPase (actomyosin-like protein) in maintaining the biconcave shape of erythrocytes

Cited by 13 publications

References 25 publications

Activation of Mg-ATPase (Spectrin-Dependent ATPase) by Ca^2+

Activation of Mg-ATPase (Spectrin-Dependent ATPase) by Ca^2+

Is there any connection between heat inactivation of spectrin‐dependent ATPase and loss of smooth biconcave shape of red cells?

Tellurite effect on ATPase activity of contractile membrane protein

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