The binding of vanadium (V) oligoanions to sarcoplasmic reticulum

Sandor VARGA, Peter CSERMELY, Anthony MARTONOSI

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)119-126
Number of pages8
JournalEuropean Journal of Biochemistry
Volume148
Issue number1
DOIs
Publication statusPublished - Apr 1985

ASJC Scopus subject areas

  • Biochemistry

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