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Distribution of parvalbumin isotypes in adult snook and their potential applications as species‐specific biomarkers
Author(s) -
Ross C.,
Tilghman R. W.,
Hartmann J. X.,
Mari F.
Publication year - 1997
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1997.tb01512.x
Subject(s) - parvalbumin , biology , ammonium sulfate precipitation , monoclonal antibody , isoelectric focusing , microbiology and biotechnology , gel electrophoresis , chromatography , biochemistry , antibody , chemistry , immunology , size exclusion chromatography , genetics , enzyme
The highly stable Ca 2+ binding protein, parvalbumin, is prevalent in fish white muscle tissue. The properties of this protein make it a promising antigen for use as a specific biomarker for fish identification. Parvalbumin was purified from white muscle of an adult common snook Centropomus undecimalis using ammonium sulfate precipitation, size‐exclusion chromatography (SEC) and anion‐exchange HPLC. Parvalbumins were characterized by the presence of an 11‐kDa band following gradient‐SDS gel electrophoresis and by their immunoreactivity against mouse anti‐parvalbumin antibodies. Anion‐exchange chromatography of the parvalbumin fraction separated from the SEC column yielded nine fractions. Subsequent analysis of these fractions by isoelectric focusing gel electrophoresis led to a total of seven parvalbumin isotypes, which may lend themselves as biomarkers in fish identification. The presence of these seven parvalbumin isotypes was confirmed independently by reversed‐phase HPLC. A dilution endpoint immunoassay was developed for C. undecimalis parvalbumin using a monoclonal antibody directed against its highly conserved calcium binding site. The utility of parvalbumin isotype distribution and specific monoclonal antibodies against fish parvalbumin in species identification is discussed.