The binding of vanadium (V) oligoanions to sarcoplasmic reticulum

The binding of vanadium (V) oligoanions to sarcoplasmic reticulum

The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can...

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Veröffentlicht in:European journal of biochemistry 1985-04, Vol.148 (1), p.119-126
Hauptverfasser: VARGA, Sandor, CSERMELY, Peter, MARTONOSI, Anthony
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Biological and medical sciences
calcium
Calcium-Transporting ATPases - antagonists & inhibitors
Calcium-Transporting ATPases - metabolism
Cell physiology
Crystallization
Fundamental and applied biological sciences. Psychology
In Vitro Techniques
Microscopy, Electron
Microsomes - metabolism
Molecular and cellular biology
Muscle contraction
Polymers - metabolism
Polymers - pharmacology
Rabbits
sarcoplasmic reticulum
Sarcoplasmic Reticulum - enzymology
Sarcoplasmic Reticulum - metabolism
Vanadates
vanadium
Vanadium - metabolism
Vanadium - pharmacology
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Zusammenfassung:The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can be rationalized in terms of one binding site per ATPase molecule for monovanadate and two sites per ATPase for decavanadate. The Ca‐ATPase crystals formed with monovanadate and with decavanadate are similar in appearance, but decavanadate is particularly effective in promoting the crystallization of Ca2+‐ATPase at low V concentration (10–100 μM) in a Ca2+‐free medium.
ISSN:0014-2956
1432-1033
DOI:10.1111/j.1432-1033.1985.tb08815.x