Covalent modification of the solubilized rat liver vitamin K-dependent carboxylase with pyridoxal-5′-phosphate

This publication has 33 references indexed in Scilit:

• Kinetics of carboxylation of endogenous and exogenous substrates by the vitamin K-dependent carboxylase
  Archives of Biochemistry and Biophysics, 1984
• Vitamin K-dependent carboxylase: Effect of detergent concentrations, vitamin K status, and added protein precursors on activity
  Archives of Biochemistry and Biophysics, 1983
• Sequence of a tryptic peptide from the NADPH binding site of the enoyl reductase domain of fatty acid synthase
  Archives of Biochemistry and Biophysics, 1983
• Vitamin K-dependent carboxylase: Requirements for carboxylation of soluble peptide substrates and substrate specificity
  Biochemical and Biophysical Research Communications, 1979
• NAD(P)H dehydrogenase and its role in the vitamin K (2-methyl-3-phytyl-1,4-naphthaquinone)-dependent carboxylation reaction
  Biochemical Journal, 1978
• Inactivation of avian progesterone receptor binding to ATP-sepharose by pyridoxal 5′-phosphate
  Biochemical and Biophysical Research Communications, 1978
• Partial sequence of rat prothrombin and the activity of two related pentapeptides as substrates for the vitamin K-dependent carboxylase system
  FEBS Letters, 1977
• Hemoglobin covalently bridged across the polyphosphate binding site
  Biochemical and Biophysical Research Communications, 1975
• Affinity labeling of the polyphosphate binding site of hemoglobin
  Biochemistry, 1972
• A specific interaction of pyridoxal 5′-phosphate and 6-phosphogluconic dehydrogenase
  Archives of Biochemistry and Biophysics, 1967