Molecular characterization of proteins in detergent solutions

来自 ACS

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摘要：

The molecular weight and Stokes radius of a protein in a detergent solution can be determined unambiguously by measurement of sedimentation equilibrium and sedimentation velocity, with analysis of the data by equations appropriate for multicomponent systems. The procedure can be simplified without much loss of accuracy by use of a calculated buoyant density factor, and detergent partial specific volumes required for this calculation have been measured. The Stokes radius can be measured independently by gel exclusion chromatography and the molecular weight can then be determined by use of sedimentation velocity alone, which is of considerable advantage since gel chromatography and sedimentation velocity do not require as high a degree of protein purity as sedimentation equilibrium. A simplified procedure for calibration of gel chromatography columns is described, and the significance and interpretation of the Stokes radius are discussed. The most important procedures have been verified by experimental measurements using the AI apoprotein of human high density serum lipoprotein in several detergent solutions.

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Humans Sodium Sodium Dodecyl Sulfate Deoxycholic Acid Enzymes Lipoproteins, HDL Peptides Proteins Apoproteins Blood Proteins