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A comparison of the physical chemical properties of oxidized and reduced alkylated ribonuclease
Authors:HARRINGTON W F  SELA M
Affiliation:1. Translational Tissue Engineering Center, Department of Biomedical Engineering and Wilmer Eye Institute, Johns Hopkins University, Baltimore, MD, USA;2. Department of Materials Science & Engineering, Johns Hopkins University, Baltimore, MD, USA;3. Biomedical Engineering Graduate Program, University of Calgary, Calgary, AB, Canada;4. Faculty of Kinesiology, University of Calgary, Calgary, AB, Canada;5. Department of Urology and Department of Chemical & Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA;1. Department of Botany, The Islamia University of Bahawalpur, Bahawalpur, 63100, Pakistan;2. Department of Botany, Government College University, Faisalabad, Pakistan;3. Department of Agronomy, Faculty of Agriculture and Environment, The Islamia University of Bahawalpur, Bahawalpur, 63100, Pakistan;4. Department of Botany, University of Agriculture, Faisalabad, Pakistan;5. Institute of Botany, University of the Punjab, Lahore, Pakistan;1. Environmental Molecular Sciences Laboratory, PNNL, Richland, 99352, WA, USA;2. Institute of Theoretical and Experimental Biophysics, Russian Academy of Science, Pushchino, 142290, Moscow Region, Russia;3. G.A. Krestov Institute of Solution Chemistry, Russian Academy of Sciences, Ivanovo, 153045, Russia
Abstract:The optical rotatory, sedimentation and viscosity properties of reduced carboxymethylated ribonuclease and oxidized ribonuclease are compared in various solvents. The solution properties of the two molecules are closely similar, suggesting that both performic acid oxidation and reduction-alkylation of the disulphide linkages lead to similar effects on the polypeptide chain configuration. Results are discussed with reference to the role of the disulphide linkages in maintaining the secondary and tertiary structure of the native enzyme.
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