Rat liver vitamin K-dependent carboxylase: a study of antibodies raised against partially purified preparations of the enzyme |
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| Authors: | R Wallin |
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| Affiliation: | 1. Department of Forensic Medicine and Toxicology, Faculty of Veterinary Medicine-Qena, South Vally University, Egypt;2. Department of Forensic Medicine and Toxicology, Faculty of Veterinary Medicine, Zagazig University, 44511 Zagazig, Egypt;3. Department of Pharmacology, Faculty of Veterinary Medicine, Qena, South Vally University, Egypt;4. Department of Animal Wealth Development, Faculty of Veterinary Medicine, Zagazig University, Egypt;1. State Key Laboratory of Heavy Oil Processing, College of New Energy and Materials, China University of Petroleum (Beijing), Beijing, 102249, China;2. Beijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, The Chinese Academy of Sciences, Beijing, 100190, China;1. Centre of Pharmacology and Toxicology, Hannover Medical School, Hannover, Germany;2. Institute of Clinical Pharmacology, Hannover Medical School, Hannover, Germany |
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| Abstract: | 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. |
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