[Quantitative analysis of polypeptides by disc electrophoresis in pore gradients].
The quantitation of components in a complex mixture of proteins of Pseudomonas denitrificans separated by disc-electrophoresis in the linear pore gradient of polyacrylamide gel was studied. The problem of a poor staining of proteins in the presence of a detergent was solved by a high resolving power photography. A linear correlation between the amount of protein in the fraction and the intensity of amide black staining was extablished. In comparison to the wild type of P. denitrificans the aldehyde negative mutant showed significant changes in protein fractions amounting to 30% of total protein, according to the densitometrical data. It is suggested that the changes are related to the protein migration in fractions rather than to an additional synthesis in different protein fractions.
D001426:Bacterial Proteins / Q000032:analysis*; D004589:Electrophoresis, Disc / Q000379:methods; D010455:Peptides / Q000032:analysis*; D011549:Pseudomonas / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate
D001426:Bacterial Proteins; D010455:Peptides; D012967:Sodium Dodecyl Sulfate
Kolichestvennyi analiz polipeptidov disk-élektroforozom v gradiente por