Isolation and immunochemical characteristics of soluble membrane proteins from the cell wall of Corynebacterium diphtheria

A method for isolation of immunochemically active proteins from Corynebacterium diphtheria membranes was elaborated. The proteins were solubilized with the nonionic detergent NP-40 and gel-filtered through an Ultrogel AcA-34 column under denaturating conditions. The purified proteins (Mr = 64 kD) we...

Full description

Saved in:
Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 52; no. 6; p. 978
Main Authors Kondrashina, N N, Shmeleva, E A, Beresten', S F
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.06.1987
Subjects
Amino Acids - analysis
Antigens, Bacterial - analysis
Cell Wall - analysis
Chromatography, Gel
Corynebacterium diphtheriae - analysis
Corynebacterium diphtheriae - immunology
Electrophoresis, Polyacrylamide Gel
Epitopes - analysis
Humans
Immunoenzyme Techniques
Membrane Proteins - analysis
Membrane Proteins - immunology
Membrane Proteins - isolation & purification
Molecular Weight
Monosaccharides - analysis
Solubility
Online AccessGet more information

Cover

More Information
Summary:A method for isolation of immunochemically active proteins from Corynebacterium diphtheria membranes was elaborated. The proteins were solubilized with the nonionic detergent NP-40 and gel-filtered through an Ultrogel AcA-34 column under denaturating conditions. The purified proteins (Mr = 64 kD) were antigenically active in a solid phase radioimmunoassay with human antidiphtheria antibodies.
ISSN:0320-9725