Rat liver vitamin K-dependent carboxylase: a study of antibodies raised against partially purified preparations of the enzyme.
Antibodies raised against three preparations of increasing purity of the microsomal vitamin K-dependent carboxylase did not neutralize essential proteins in the enzyme complex. When immobilized on Sepharose the antibodies removed 75% of contaminating proteins in the starting material, including cytochrome P-450. Immunoaffinity chromatography was more efficient when carried out in the presence of the detergent CHAPS than in the presence of Triton X-100. Immunoabsorption stimulated carboxylase activity 2.9-fold and resulted in a 66-fold increase in the specific activity of the complex.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D019735:Carbon-Carbon Ligases; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007074:Immunoglobulin G / Q000302:isolation & purification; D007700:Kinetics; D008025:Ligases / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D009994:Osmolar Concentration; D051381:Rats; D011919:Rats, Inbred Strains
D000906:Antibodies; D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D008025:Ligases; D019735:Carbon-Carbon Ligases; C020660:glutamyl carboxylase