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sodium dodecyl sulfate-polyacrylamide gel electrophoresis

Time:2015/11/28 5:52:46

Direct detection of an antimicrobial peptide of Pediococcus acidilactici in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. J. Ind. Microbiol., 2, 319-322

ABSTRACT An SDS-PAGE technique is described that allows identification of the antimicrobial activity of a peptide secreted by a strain ofPediococcus acidilactici. This peptide has an antimicrobial property against several baeteria associated with food. This technique enables detection of the specific peptide (or protein) band(s) associated with the inhibitory effect which can then be eluted from the gel for further studies.

Behavior of glycopolypeptides with empirical molecular weight estimation methods. 1. In sodium dodecyl sulfate.

The influence of the presence of oligosaccharide branches was examined with respect to the behavior of glycopolypeptides in empirical molecular weight estimation methods in the presence of sodium dodecyl sulfate (NaDodSO4). This examination was conducted by comparing the gel chromatographic and gel electrophoretic behaviors in the presence of NaDodSO4 of 13 glycopolypeptides of known chemical and physical properties to those of regular polypeptides. Errors in the gel chromatographic molecular weight for glycopolypeptides in NaDodSO4 varied from -22% to +10% and indicated that the hydrodynamic behavior of the glycopolypeptide--NaDodSO4 complex could not be correlated with the amount of carbohydrate in the glycopolypeptide. NaDodSO4 binding measurements on a number of the glycopolypeptides suggest that the polypeptide moiety binds the nominal weight ratio of NaDodSO4, while the carbohydrate portion exhibits little or no NaDodSO4 binding. As has been reported by others, the polyacrylamide gel electrophoretic behavior of glycopolypeptide--NaDodSO4 complexes yielded abnormally high molecular weight estimates. In general, the error of these estimates diminished with decreasing porosity of the gel; however, each glycopolypeptide behaved in a unique fashion. Treatment of the electrophoretic data by any of several empirical means provided no reliable way to correct for the glycopolypeptides' aberrant behavior