Abstract
The polycondensation of hemoglobin and serum albumin with glutaric aldehyde has been investigated, varying pH values and the components concentrations. On the basis of a study of MW levels of the products the influence of protein charges on the formation of oligomers has been determined. The hydrodynamic properties and morphology of oligomers of the proteins have been investigated by methods of electrophoresis in PAAG in the presence of sodium dodecyl sulphate and sedimentation diffusion analysis. It was found that oligomers at the level of hemoglobin tetramers have a compact structure approximating to a globular one. The compact arrangement of protein molecules in oligomer has been substantiated by the results of low-angle X-ray scattering analysis.
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