Probing the catalytic subunit of the tonoplast H+-ATPase from oat roots. Binding of 7-chloro-4-nitrobenzo-2-oxa-1,3,-diazole to the 72-kilodalton polypeptide.

This publication has 45 references indexed in Scilit:

• Decrease of pH Gradients in Tonoplast Vesicles by NO₃⁻ and Cl⁻: Evidence for H⁺-Coupled Anion Transport
  Plant Physiology, 1987
• Potential-Dependent Anion Transport in Tonoplast Vesicles from Oat Roots
  Plant Physiology, 1987
• Solubilization and purification of the ATPase from the tonoplast of Hevea
  European Journal of Biochemistry, 1985
• Partial purification and characterization of an anion-activated ATPase from radish microsomes
  European Journal of Biochemistry, 1985
• Anion-Sensitive, H⁺-Pumping ATPase in Membrane Vesicles from Oat Roots
  Plant Physiology, 1983
• The Proton‐Translocating Adenosine Triphosphatase of the Obligately Anaerobic Bacterium Clostridium pusteuriunum
  European Journal of Biochemistry, 1979
• Reaction of (sodium(1+)-potassium(1+) ion)-activated ATPase with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole: evidence for an essential tyrosine at the active site
  Biochemistry, 1978
• The Mitochondrial ATPase
  European Journal of Biochemistry, 1975
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• The reactivity of SH groups with a fluorogenic reagent
  FEBS Letters, 1970