Numerical analysis of normalized whole-cell protein profiles after sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

A technique is described for mathematically normalizing whole-cell protein profiles after sodium dodecyl sulphate-polyacrylamide gel electrophoresis to obtain standardized absolute migration distances using two internal Mr standards. A soft laser scanning densitometer was used to measure protein band migration distances in wet, silver-stained gels. The normalized values were superior to the unnormalized migration distances and common RF values in reducing the inter- and intragel variability of the protein band positions. A procedure is described for clustering normalized bacterial protein profiles using a sample data set obtained from the type strains of four Legionella species.