Abstract
Horizontal two-dimensional gel electrophoresis with immobilized pH gradients in the first dimension resulted in excellent patterns of porcine erythrocyte lysate proteins. The overwhelming excess of hemoglobin was removed by chloroform-ethanol extraction and the number of spots further increased by acetone precipitation, revealing considerably more protein spots than detected by analyzing the untreated sample. A total of 430 protein spots have been reproducibly obtained for further analysis of genetic variations. A number of enzyme systems have been identified by visual inspection and comparison with previous results. The existence of further multiple forms for other enzymes is also apparent.
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