The binding of vanadium (V) oligoanions to sarcoplasmic reticulum.
نویسندگان
چکیده
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 microM) in a Ca2+-free medium.
منابع مشابه
51V-n.m.r. analysis of the binding of vanadium(V) oligoanions to sarcoplasmic reticulum.
The binding of mono- and oligo-vanadates to sarcoplasmic reticulum was analysed by 51V-n.m.r. spectroscopy. The observations indicate that, in addition to monovanadate, the di-, tetra- and deca-vanadates are also bound to sarcoplasmic-reticulum membranes with high affinity. The binding of the vanadate oligoanions may explain some of the effects of vanadates on the conformation and crystallizati...
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عنوان ژورنال:
- European journal of biochemistry
دوره 148 1 شماره
صفحات -
تاریخ انتشار 1985