Cyanate formation and electrophoretic behavior of proteins in gels containing urea |
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| Authors: | E G Cole D K Mecham |
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| Affiliation: | 1. Department of Chemistry and Applied Bioscience, ETH Zurich, Zurich, Switzerland;2. YPSO-FACTO, 10 Viaduc Kennedy, 54000 Nancy, France;1. Department of Chemistry and Biochemistry, South Dakota State University, Avera Health and Science, Box 2202, Brookings, SD 57007, United States of America;2. MRIGlobal, 425 Volker Boulevard, Kansas City, MO 64110-2241, United States of America;3. Pediatrics-Pulmonary Medicine, University of Colorado-Denver, Denver, CO, 80045, United States of America;1. Department of Molecular Genetic Diagnostics and Cell Biology, Division of Laboratory Medicine, Institute of Pediatrics, Research Center for Children''s Health, 119991 Moscow, Russia;2. Institute of General Pathology and Pathophysiology, Russian Academy of Medical Sciences, Moscow 125315, Russia;3. Institute for Atherosclerosis Research, Skolkovo Innovative Center, Moscow 121609, Russia;4. Faculty of Medicine, School of Medical Sciences, University of New South Wales, Sydney, NSW 2052, Australia;5. School of Medicine, University of Western Sydney, Campbelltown, NSW 2560, Australia |
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| Abstract: | Exposure to cyanate in urea solutions and the resulting carbamylation of amino groups in some components may change the patterns given by protein mixtures upon electrophoresis in starch or polyacrylamide gels as shown by the behavior of water-soluble proteins from wheat flour and crude casein. Depending upon the specific component and the degree of exposure to cyanate, new (artifact) bands may appear in the pattern or the sharpness of bands may be obscured. Procedures to minimize exposure to cyanate in the use of horizontal electrophoresis with polyacrylamide gels are described. |
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