A procedure developed involved isoelectrofocusing in borate-polyol system and thin-layer electrophoresis in polyacrylamide gel gradient containing sodium dodecylsulfate of the products of human blood serum albumin obtained after partial hydrolysis. The first dimension isoelectrofocusing in borate-polyol system allowed to separate peptides with close values of pI and to increase the procedure sensitivity. The procedure may be recommended for identification of proteins, for estimation of the protein degradation in hydrolysis as well as for studies of peptide maps of albumin under normal and pathological states.
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