Beef liver glutamate dehydrogenase: A study of the oxidation of various alternative amino acid substrates retaining the correct spacing of the two carboxylate groups

This publication has 22 references indexed in Scilit:

• Kinetic studies to determine the mechanism of regulation of bovine liver glutamate dehydrogenase by nucleotide effectors
  Biochemistry, 1982
• The preparation of pure salt-free nicotinamide coenzymes
  Analytical Biochemistry, 1977
• The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate
  Biochemical Journal, 1977
• Protection of glutamate dehydrogenase by nicotinamide–adenine dinucleotide against reversible inactivation by pyridoxal 5′-phosphate as a sensitive indicator of conformational change induced by substrates and substrate analogues
  Biochemical Journal, 1974
• Kinetic measurements with monocarboxylic acids as substrates and effectors of glutamate dehydrogenase
  FEBS Letters, 1972
• Active centre equivalent weight of glutamate dehydrogenase from dry weight determinations and spectrophotometric titrations of abortive complexes
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
• Nonlinear kinetics of glutamate dehydrogenase. Studies with substrates-glutamate and nicotinamide-adenine dinucleotide
  Biochemistry, 1971
• Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes
  Biochemical Journal, 1969
• γ-Methyleneglutamic acid and related compounds from plants
  Biochemical Journal, 1964
• Preparation of β-Methylglutamic Acid¹
  Journal of the American Chemical Society, 1955