Dissociation-Association of lactate dehydrogenase Isozymes: Influences on the formation of tetramers versus dimers of M4-LDH and H4-LDH

This publication has 15 references indexed in Scilit:

• The dimeric intermediate on the pathway of reconstitution of lactate dehydrogenase is enzymatically active
  FEBS Letters, 1983
• H4-isozyme of lactate dehydrogenase in a solution of sodium c chloride—6. The effect of oxalate and oxamate on the molecular weight
  International Journal of Biochemistry, 1982
• H4-isozyme of lactate dehydrogenase in the solution of sodium chloride—II the effect of ADP-ribose on the molecular weight
  International Journal of Biochemistry, 1982
• H4-isozyme of lactate dehydrogenase in a solution of sodium chloride—I. The molecular weight of H4-lactate dehydrogenase in relation to sodium chloride concentration, enzyme concentration and temperature
  International Journal of Biochemistry, 1982
• Analysis of the reconstitution of oligomeric enzymes by crosslinking with glutaraldehyde: kinetics of reassociation of lactic dehydrogenase
  Biochemistry, 1981
• Molecular Properties of Lactic Dehydrogenase under the Conditions of the Enzymatic Test
  European Journal of Biochemistry, 1973
• Factors affecting tetramer dissociation of rabbit muscle lactate dehydrogenase and reactivity of its sulfhydryl groups
  Biochemistry, 1973
• Substrate-inhibited lactate dehydrogenase. Reaction mechanism and essential role of dissociated subunits
  Biochemistry, 1970
• Kinetics of Rabbit Muscle Lactate Dehydrogenase over a Large Concentration Range
  Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1970
• Reversible dissociation of enzymes at high dilutions and their inhibition by polyanions
  Archives of Biochemistry and Biophysics, 1965