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Quantification of azo-coupled lysine in azo proteins by amino acid analysis
Authors:G J Pielak  S Gurusiddaiah  J I Legg
Affiliation:1. Department of Biochemistry, University of British Columbia, Vancouver, British Columbia, Canada V6T 1W5;2. Department of Chemistry and Program in Biochemistry, Washington State University, Pullman, Washington 99164-4630 USA;1. Department of Geological Sciences, University of Florida, Gainesville, FL 32611, United States of America;2. United States Geological Survey, Geology, Geophysics, Geochemistry Science Center, Denver, CO 80225, United States of America;3. Department of Geology and Geophysics, Woods Hole Oceanographic Institution, Woods Hole, MA 02543, United States of America;4. Department of Geosciences, Boise State University, Boise, ID 83725, United States of America
Abstract:Hydrochloric acid hydrolysis of azo proteins in which lysine residues are azo coupled, results in conversion of modified lysines to alpha-amino-epsilon-hydroxy caproic acid plus alpha-amino-epsilon-chloro caproic acid. The latter can interfere with the determination of tyrosine by amino acid analysis. This potential problem can be avoided either by making basic and then neutralizing HCl hydrolysates or by hydrolyzing the protein in methane sulfonic acid.
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