Nonenzymatic Modifications to Keratins by

An example of the effects of aldehydic changes was obtained by monitoring the effect of ethanol ingestion on the keratin taken from rat hair (JelfnkovA et al., 1995). In this study CE profiles of hair keratins taken from rats fed 10% ethanol and from rats fed water were compared by single-dimension 

Further characterization of the remaining fraction in the low-sulfur keratin group in the ethanol-treated animals included analysis of the trypsin-released peptides by plasma desorption mass spectrometry. These results indicated the 

The foregoing analysis makes clear that capillary electrophoresis can reveal differences in keratin proteins obtained from animals treated with ethanol compared to controls. However, it is also apparent that because of the complexity of the protein matrix, other methods must be used as well to identify the modified fraction. 

CZE offers the potential of ultramicroanalyses of enzymatic activities in biological samples. This application could be useful in forensic cases when only trace amounts of biological specimens are available—for example, in the detection of amylase activity from saliva extracted from stamps or envelopes. 

When the substrate and the enzyme are electrophoretically mixed, most of the enzyme will appear in the enzyme-substrate complex. Returning to the example used by Bao and Regnier, the net charge of the enzyme-substrate complex will be 10 - 2 = 8. Since enzyme activity measurements are performed under substrate-saturating conditions, all the enzyme will be bound to substrate, and the mobility of the enzyme should be the mobility of the ES complex. 

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