Abstract

Bovine mercaptalbumin has been modified at the carboxyl groups by means of 1-ethyl-3 (3-dimethylisopropyl) carbodiimide and glycine amide. A stable derivative was obtained after modification of 54 groups. The modified protein differed only slightly from the unmodified one with respect to the optical rotatory dispersion parameters ao, bo and χc. This preparation was studied in the analytical ultracentrifuge in a CsCl gradient in the pH-interval from 2 to 11. The buoyant densities were determined and compared with those of the unmodified protein in the same pH-interval. The contribution from the carboxyl groups to the buoyant density is discussed and compared with results obtained with other proteins and synthetic polypeptides.

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