PMID: 37435May 1, 1977

Cooperative interaction of serum albumin with quaternized poly-4-vinyl pyridine and structure of the complexes

Molekuliarnaia biologiia
V A KabanovA D Antipina

Abstract

Interaction of bovine serum albumin (BSA) with quaternized poly-4-vinyl pyridine (PE) in aqueous solutions at pH 7 was studied. It was shown that in a wide range of the ratios of the components (nBSA/nPE) soluble stable cooperative complexes were formed. At the same time a certain critical content of the protein exists at which the system loses its homogeneity. Complex formation is not accompanied by protein denaturation. At smaller nBSA/nPE ratios non-homogeneous distribution of protein globulas among polyelectrolite macromolecules was found; this corresponded to the "all or none" principle. Using ultracentrifugation technique viscosimetric measurements and electron microscopy it was shown that the soluble complexes exist in the form of rode-like particles consisting of protein globules stabilized by polycation chains. Such particle can be considered as a model of nucleoprotein complex. At certain crytical nBSA/nPE rations the rod-like particles aggregate with additional number of BSA-molecules and form more complicate soluble and insoluble cooperative complexes. Possible structural models of the complexes described were suggested and the thermodinamic and kinetic cryteria of their self-assembly were discussed.

Related Concepts

Serum Albumin Measurement
Nucleoproteins
Complex (molecular entity)
ALB
Plasma Protein Binding Capacity
Viscosity
Soluble
Electron Microscopy, Diagnostic
Macromolecule
Protein Conformation

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