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Separation and Characterization of a Porcine‐specific Thermostable Muscle Protein from Cooked Pork
Author(s) -
Chen F.C.,
Hsieh YH.P.
Publication year - 2001
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2001.tb15175.x
Subject(s) - thermostability , isoelectric focusing , chemistry , isoelectric point , monoclonal antibody , chromatography , biochemistry , affinity chromatography , ion chromatography , antigen , antibody , biology , enzyme , genetics , immunology
This study was undertaken to separate and characterize the porcine‐specific thermostable muscle protein (psTSMP) recognized by monoclonal antibody, MAb 5H9, which was previously raised against crude porcine thermostable muscle proteins for detection of pork in cooked meats. The 24 kD antigenic components isolated from cooked pork by immunoaffinity chromatography consisted of a basic protein (pI = 9.4) and a group of isoelectric variants (pI ranging from 5.4 to 7.2). The basic protein was further isolated by methyl hydrophobic interaction and sulfonate ion‐exchange chromatography. Immunoblot suggested the presence of this antigenic psTSMP in the tropo‐nin fraction. Based on its molecular weight, pI, thermostability, and immunoreactivity, the psTSMP was tentatively identified as troponin I.