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[Conformational stability and immunochemical properties of yersinin--a basic protein of the outer membrane of the Pseudotuberculosis microbe].

Authors
Type
Published Article
Journal
Bioorganicheskaia khimiia
Publication Date
Volume
15
Issue
6
Pages
763–772
Identifiers
PMID: 2675850
Source
Medline
License
Unknown

Abstract

Using spectroscopic methods (circular dichroism and intrinsic protein fluorescence) and immunoenzyme assay, changes in the spatial and antigenic structure of yersinin, porin from outer membrane of Yersinia pseudotuberculosis, were studied in solutions of ionic and non-ionic detergents at various temperatures and low pH values. Yersinin was shown to retain its secondary structure under various denaturation conditions, the content of regular structural patterns depending on specific action of the denaturation agent. Process of yersinin denaturation similarly to other membrane proteins appears to occur via two structural transitions: dissociation of oligomers and denaturation of monomers. At the first stage changes of quaternary structure accompanied by the loss of so called conformational determinants were observed. Temperature-dependent changes of monomers' tertiary structure affect antigenic activity of yersinin in a smaller degree.

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