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Acrylamide in Polyacrylamide Gels Can Modify Proteins during Electrophoresis

โœ Scribed by C. Bonaventura; J. Bonaventura; R. Stevens; D. Millington


Book ID
102559271
Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
368 KB
Volume
222
Category
Article
ISSN
0003-2697

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โœฆ Synopsis


Many notable discoveries have resulted from the characterization or purification of compounds by electrophoresis. The results reported here show that when polyacrylamide gels are used as the support matrix for electrophoresis, proteins can be modified by reaction with unpolymerized monomers of acrylamide, forming covalent acrylamide adduction products. This was demonstrated by electrophoresis of human and rat hemoglobins and subsequent analysis by electrospray ionization mass spectrometry. The degree of covalent acrylamide binding can be appreciable. The degree of adduction is dependent upon the condition of the gel matrix, the amount of material applied, and the reactivity of the material under investigation. (1994 Academic Press, Inc.


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The recovery of proteins in polyacrylamide gel electrophoresis (PAGE) has not been previously investigated systematically. The fractionation of hemoglobins A and 8 (1) by which milligram-preparative PAGE (2) was initially introduced yielded nearly quantitative recovery of hemoglobin, a finding which