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Determination of relative amounts of silver stained proteins on two‐dimensional gels using internal calibrator

Proteins separated by isoelectric focusing of 20 samples and polyacrylamide gel electrophoresis of 10 samples in the same batch were stained with silver and were scanned with a computerized laser beam densitometer to obtain integrations values. A linear relationship was found between densitometric integration values (staining intensities) of proteins and their loads up to 600 ng (actin, carbonic anhydrase) or 1000 ng (albumin, creatine kinase), respectively. The same amount (250 ng) of applied albumin, actin, carbonic anhydrase and creatine kinase resulted in differences in staining intensities of these proteins; staining intensities of albumin and creatine kinase were similar, however: both were 1.8 X higher than the staining intensity of carbonic anhydrase and 2.3 X higher than of actin. Six human aortic intima proteins (ML‐1, ML‐2, P27, −14, P27,−18, P27,−19.5, P110) were selected for quantitative studies of the relationship between loads of intimal extract and the integration values of these proteins. Linear responses were found for these proteins in loads from 5 μL to 20 μL of intimal extract, corresponding approximately from 15 μg to 60 μg of total proteins applied to the focusing gel. When carbonic anhydrase was included with each sample, as an internal absorbance calibrator, we could express integration values of other proteins in relative amount in ng of carbonic anhydrase and thus compensate for variation in fixation, developing and staining conditions from batch to batch.