Partial purification of horse‐specific soluble muscle proteins by immunoadsorption chromatography

ArticleinJournal of the Science of Food and Agriculture 58(3):447 - 449 · January 1992with11 Reads
Impact Factor: 1.71 · DOI: 10.1002/jsfa.2740580323

    Abstract

    Immunoadsorption chromatography has been used to isolate horse-specific soluble muscle proteins from crude horse protein extracts. Horse-specific polyclonal antibodies against soluble horse muscle proteins immobilised on a Protein A-Sepharose CL-4B matrix were used to adsorb the corresponding antigens. Analysis of the crude soluble horse muscle proteins by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) showed the existence of 20 protein subunits in the gel. SDS-PAGE of the proteins recovered by affinity chromatography showed nine protein subunits, three of which were enriched after the immunopurification step. These affinity-recovered horse-specific soluble muscle proteins may be used as antigens in the development of monoclonal antibodies to detect and quantify horse meat in raw, unheated meat mixtures.