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

Departamento de Nutrición y Bromatología III (Higiene y Tecnología de los Alimentos), Facultad de Veterinaria, Universidad Complutense, 28040 Madrid, Spain
Journal of the Science of Food and Agriculture (Impact Factor: 1.88). 09/2006; 58(3):447 - 449. 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.