Uncoupling of Ca2+ transport in sarcoplasmic reticulum as a result of labeling lipid amino groups and inhibition of Ca2+-ATPase activity by modification of lysine residues of the Ca2+-ATPase polypeptide.

This publication has 24 references indexed in Scilit:

• Highly purified sarcoplasmic reticulum vesicles are devoid of Ca2+-independent (‘basal’) ATPase activity
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1980
• The effect of calcium oxalate crystallization kinetics on the kinetics of calcium uptake and calcium ATPase activity of sarcoplasmic reticulum vesicles
  Cell Calcium, 1980
• Inhibition of calcium transport in sarcoplasmic reticulum after modification of highly reactive amino groups
  Biochemical and Biophysical Research Communications, 1980
• Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum
  Annual Review of Biochemistry, 1979
• Localization of the amino phospholipids in sarcoplasmic reticulum membranes revealed by trinitrobenzene-sulfonate and fluorodinitrobenzene
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1977
• Sarcoplasmic reticulum adenosine triphosphatase: Labeling of an essential lysyl residue with pyridoxal-5′-phosphate
  Archives of Biochemistry and Biophysics, 1977
• Calcium Transport in Sarcoplasmic Reticulum
  Annual Review of Biophysics and Bioengineering, 1975
• Reversible lipid titrations of the activity of pure adenosine triphosphatase-lipid complexes
  Biochemistry, 1974
• Reconstitution of a Calcium Pump Using Defined Membrane Components
  Proceedings of the National Academy of Sciences, 1974
• Novel reagent for the fluorometric assay of primary amines
  Journal of the American Chemical Society, 1972