Abstract
Abstract The hepta-, octa- and decapeptides, angiotensins III, II, and I with molecular weights 930, 1,045, and 1,295, were separated by polycrylamide pel electrophoresis at pH 6.41, positive polarity, using gel concentrations ranging from 24 to 40 %T, 2 %CBis. The peptides were detected by a conventional protein staining method using Cooraassie Brilliant Blue R-250 modified by the addition of 1.25% glutaraldehyde, thus crosslinking the peptides to “proteins”. Separation between the 3 peptides Is due nearly entirely to net charge rather than to size. Resolution is therefore optimal in charge fractionatton methods such as electrofocusing, chromatofocusing, ion exchange chromatography and liquid-liquid partition chromatography.
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