1984International Journal of Food Science & TechnologyRequires access

Detection and partial characterization of soluble pig muscle proteins by immunoelectrophoresis in agarose gels

Carmen Casás, J. Tormo, Pablo E. Hernández, B. Sanz

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Abstract

Abstract Immunoelectrophoresis in agarose gels has been used to detect and partially characterize specific protein precipitin bands of soluble proteins of pig muscle (PSP), free of cross-reactions with soluble muscle proteins of cow (CSP), horse (HSP) and chicken (CHSP). Out of six precipitin bands obtained by reacting PSPs against an anti-PSP antiserum produced by a rabbit, four bands were observed to appear by reacting HSPs against the same anti-PSP antiserum. Two more bands were detected by analysing CSPs against an anti-PSP antiserum and three bands were detected by analysing CHSPs against the same anti-PSP antiserum. Thus, only one band is specific to the soluble protein of pig muscle. This technique may have the potential to detect the presence of pork in unheated ground meat products.

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Abstract Immunoelectrophoresis in agarose gels has been used to detect and partially characterize specific protein precipitin bands of soluble proteins of pig muscle (PSP), free of cross-reactions with soluble muscle proteins of cow (CSP), horse (HSP) and chicken (CHSP). Out of six precipitin bands obtained by reacting PSPs against an anti-PSP antiserum produced by a rabbit, four bands were observed to appear by reacting HSPs against the same anti-PSP antiserum. Two more bands were detected by analysing CSPs against an anti-PSP antiserum and three bands were detected by analysing CHSPs against the same anti-PSP antiserum. Thus, only one band is specific to the soluble protein of pig muscle. This technique may have the potential to detect the presence of pork in unheated ground meat products.

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Available abstract

Abstract Immunoelectrophoresis in agarose gels has been used to detect and partially characterize specific protein precipitin bands of soluble proteins of pig muscle (PSP), free of cross-reactions with soluble muscle proteins of cow (CSP), horse (HSP) and chicken (CHSP). Out of six precipitin bands obtained by reacting PSPs against an anti-PSP antiserum produced by a rabbit, four bands were observed to appear by reacting HSPs against the same anti-PSP antiserum. Two more bands were detected by analysing CSPs against an anti-PSP antiserum and three bands were detected by analysing CHSPs against the same anti-PSP antiserum. Thus, only one band is specific to the soluble protein of pig muscle. This technique may have the potential to detect the presence of pork in unheated ground meat products.

Key concepts: Antiserum, Precipitin, Agarose, Immunoelectrophoresis, Chemistry, Biochemistry, Electrophoresis, Molecular biology

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