Chapter 4 Molecular Size and Shape in Electrophoresis

作者: Z. Deyl

DOI: 10.1016/S0301-4770(08)60880-5

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摘要: Publisher Summary The molecular charge has no influence on net migration in electrophoresis, if the pore and diameters are identical. In order to decrease scatter of data, it is necessary find a suitable means eliminating differences among different separated species. If an electrophoretic separation carried out gel that size small enough restrict mobility, relationship between distance travelled by particular zone its weight nearly linear. Proteins with higher weights more retarded matrix compared those lower weights. Good results can be obtained within average values weight. It was noticed at beginning development sodium dodecyl sulphate (SDS) procedure addition SDS proteins under conditions which denaturation does not occur, native conformation protein remains preserved even after detergent been added. optical rotatory dispersion (ORD) spectra revealed preservation considerable amount structures, such as a-helix SDS.

参考文章(36)
W. H. Evans, J. W. Gurd, Preparation and properties of nexuses and lipid-enriched vesicles from mouse liver plasma membranes Biochemical Journal. ,vol. 128, pp. 691- 700 ,(1972) , 10.1042/BJ1280691
Jacqueline A. Reynolds, Charles Tanford, The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes Journal of Biological Chemistry. ,vol. 245, pp. 5161- 5165 ,(1970) , 10.1016/S0021-9258(18)62831-5
A K Dunker, R R Rueckert, Observations on Molecular Weight Determinations on Polyacrylamide Gel Journal of Biological Chemistry. ,vol. 244, pp. 5074- 5080 ,(1969) , 10.1016/S0021-9258(18)94310-3
Billy G. Hudson, Robert G. Spiro, Studies on the Native and Reduced Alkylated Renal Glomerular Basement Membrane Journal of Biological Chemistry. ,vol. 247, pp. 4229- 4238 ,(1972) , 10.1016/S0021-9258(19)45065-5
Hartmut Glossmann, David M. Neville, Glycoproteins of Cell Surfaces A COMPARATIVE STUDY OF THREE DIFFERENT CELL SURFACES OF THE RAT Journal of Biological Chemistry. ,vol. 246, pp. 6339- 6346 ,(1971) , 10.1016/S0021-9258(18)61794-6
Klaus Weber, David J. Kuter, Reversible Denaturation of Enzymes by Sodium Dodecyl Sulfate Journal of Biological Chemistry. ,vol. 246, pp. 4504- 4509 ,(1971) , 10.1016/S0021-9258(18)62040-X