Lysozyme electrophoresis samples

Continuous free flow electrophoresis has been used for the separation of biopolymers (e.g. ovalbumin and lysozyme) [20] as well as smaller inorganic species (e.g. [Co sepulchrate)] and [Co (CN)g] ) [21]. Sample processing rates of 15 mg h were reported for a mixture of Amaranth (MW 804) and Patent Blue VF (MW 1159) [22]. 

In order to analyse the properties of the inactivated lysozyme, the enzyme was subjected to further analysis by electrophoresis and chromatography. Both analyses of the samples at various pHs, inactivated to the extent over 95%, indicated that the product is composed of one peak. The ozonized lysoz3mie moved slower than the native lysozyme on DEAE-Sephadex and the products at different pHs were readily distinguished from each other (Fig, 3), However, a diffuse band was observed for ozonized lysozyme as distinct from a sharp band for native lysozyme in polyacrylamide gel (17), The presence of only one band suggests that the ozonolysis does not cause the cleavage of peptide bonds and the remaining activity is not due to the presence of a small amount of unmodified lysozyme. 

Figure 2. The polypeptide chains of human cathepsin D. The samples run in electrophoresis in the presence of sodium dodecyl sulphate were (a) molecular weight markers, ovalbumin (43,000), carbonic anhydrase (29,000) and chicken lysozyme (14,300) (b) 3-form of human cathepsin D treated with mer-captoethanol (c) 3-form of human cathepsin D treated with iodoacetate. The direction of migration was downward, in an electrophoretic system similar to that of Alvares and Seikevitz (24). Doublets at about 30,000 and 14,000 molecular weight indicate that there are two bonds close together in the molecule susceptible to cleavage. No uncleaved molecules were detected in the region of 43,000 molecular weight.

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