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STRUCTURAL CHANGES BETWEEN BEEF OXY‐ AND METMYOGLOBIN AS REVEALED BY MONOCLONAL ANTIBODIES
Author(s) -
LEVIEUX A.,
LEVIEUX D.
Publication year - 1995
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1995.tb00545.x
Subject(s) - metmyoglobin , myoglobin , chemistry , monoclonal antibody , biochemistry , biotinylation , antibody , chromatography , medicine , immunology
Oxy‐ and metmyoglobin were purified from beef muscle using ion‐exchange chromatography on Mono‐Q. Their reactivity against six monoclonal antibodies (MAbs) to beef myoglobin was compared in a competitive ELISA using biotinylated beef oxymyoglobin. Four MAbs reacted with higher affinity for oxymyoglobin than for metmyoglobin. A similar higher reactivity of oxymyoglobin versus metmyoglobin was obtained with a sandwich ELISA using peroxidase‐labelled rabbit anti‐serum against beef myoglobin. Such a result has never been reported for myoglobins of any species. These MAbs should be valuable tools for analyzing conformational changes of oxymyoglobin solutions when subjected to chemical or physical treatments.