초록

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Abstract ▼ AI-Helper

Plasma albumin was purified from the fresh bovine blood using a minor modification of the polyethyleneglycol and ethanol procedure. The resulting protein solution was tested for its purity by both electrophoretic and immunochemical methods and found to contain only the albumin molecules. Each of the...

Plasma albumin was purified from the fresh bovine blood using a minor modification of the polyethyleneglycol and ethanol procedure. The resulting protein solution was tested for its purity by both electrophoretic and immunochemical methods and found to contain only the albumin molecules. Each of the four thiol reagents, maleate, iodoacetate, iodoacetamide and glutathione, was incubated with the purified plasma albumin. The electrophoresis on cellulose acetate of those complexes in various buffers with different component and pH demonstrated that the albumin-glutathione complex was separated into two zones in all buffers used except the barbital and sodium acetate buffers, that the complexes of albumin-iodoacetate and albumin-iosoacetamide also into two zones only in pH 4.8 citrate buffer and in pH 4.8 succinate buffer and that the new zone had more positive net charge compared to the native protein in any case. These results might suggest a possibility that the electrophoretic albumin fraction is composed of at least two molecular species with different conformation.