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Amino acid spacing in isotachophoresis on polyacrylamide gel: A critical evaluation by Nga Y. Nguyen; Andreas Chrambach is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Isotachophoresis of colored model proteins was carried out on polyacrylamide gel, using the stack of a multiphasic buffer system computed on the basis of the Jovin theory and operative at pH 10.4. The stack was elongated by milligram loads of various amino acids per analytical gel. The extent of the stack was determined by chemical localization of the leading and trailing constituents. The isotachophoretic nature of the stack was ascertained by determining the positions of all protein species under study as intermediate between the leading and trailing constituents. The shallow pH gradient across the extended stack was measured. Spacing of proteins in isotachophoresis is restricted, with regard to constituent multiplicity and constituent load, by the practical limitations of electrophoresis time and gel length. Therefore, spacing by a small number of constituents at relatively low loads was attempted. Amino acids were chosen as spacers because they can be selected conveniently, in radioactively labeled form, for the specific separation between pairs of proteins with particular mobilities. In the particular buffer system used, lysine, histidine, serine, and threonine were found to b

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Author

Nga Y. Nguyen; Andreas Chrambach

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

1979

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)