Controlled proteolysis of the purified Ca2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme.

This publication has 41 references indexed in Scilit:

• Purified red blood cell Ca2+-pump ATPase: Evidence for direct inhibition by presumed anti-calmodulin drugs in the absence of calmodulin
  Cell Calcium, 1982
• The anticalmodulin drugs trifluoperazine and R24571 remove the activation of the purified erythrocyte Ca²⁺‐ATPase by acidic phospholipids and by controlled proteolysis
  FEBS Letters, 1982
• Inhibition of the purified and reconstituted calcium pump of erythrocytes by μM levels of dids and nap‐taurine
  FEBS Letters, 1982
• Purification of (Ca²⁺ + Mg²⁺‐ATPase from smooth muscle by calmodulin affinity chromatography
  FEBS Letters, 1981
• Modulation of human erythrocyte Ca2+Mg2+ ATPase activity by phospholipase A2 and proteases. A comparison with calmodulin
  Biochemical and Biophysical Research Communications, 1980
• Activation of myosin light chain kinase by trypsin
  Biochemical and Biophysical Research Communications, 1980
• Calcium-dependent affinity chromatography of calmodulin on an immobilized phenothiazine
  Biochemical and Biophysical Research Communications, 1979
• Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: Its similarity to the activator of 3′:5′ — cyclic nucleotide phosphodiesterase
  Biochemical and Biophysical Research Communications, 1977
• Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase
  Biochemical and Biophysical Research Communications, 1977
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970