Abstract
Proteins from frozen histological sections of human muscle were analyzed by two-dimensional gel electrophoresis. Patterns so obtained were identical to those from whole homogenates of muscle prepared from frozen tissue powders that had much higher protein concentrations. To increase the number of proteins visible on gels of samples low in protein content, the gels were silver stained, or the proteins were labeled with [14C]iodoacetamide before electrophoresis and the gels were fluorographed. The latter method allow use of a single frozen-tissue section for two-dimensional electrophoretic analysis and brings the technique closer to practicable clinical use.

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