Literature DB >> 9435120

Development of a capillary zone electrophoresis method for caseinoglycomacropeptide determination.

S Cherkaoui1, N Doumenc, P Tachon, J R Neeser, J L Veuthey.   

Abstract

Caseinoglycomacropeptide (CGMP) is a polypeptide of 64 amino acid residues, derived from the C-terminal part of bovine kappa-casein. A sensitive and selective capillary zone electrophoresis method has been developed and validated for the analysis and quantitation of CGMP. Separation is carried out at 30 kV, using an uncoated fused-silica capillary and 20 mM sodium citrate buffer at acidic pH 3.5. The described method allows the separation of various CGMP subcomponents. The validation data proves that the method has the requisite selectivity, sensitivity, reproducibility and linearity for CGMP assay and for quality control during CGMP manufacturing (batch-to-batch reproducibility).

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Year:  1997        PMID: 9435120     DOI: 10.1016/s0021-9673(97)00756-5

Source DB:  PubMed          Journal:  J Chromatogr A        ISSN: 0021-9673            Impact factor:   4.759


  2 in total

1.  A highly sensitive sandwich ELISA for the determination of glycomacropeptide to detect liquid whey in raw milk.

Authors:  Norma A Chávez; Juan Jauregui; Laura A Palomares; Karla E Macías; Mariela Jiménez; Eva Salinas
Journal:  Dairy Sci Technol       Date:  2012-01-18

2.  Chemical and functional properties of glycomacropeptide (GMP) and its role in the detection of cheese whey adulteration in milk: a review.

Authors:  Rajan Sharma; Yudhishthir Singh Rajput; Bimlesh Mann
Journal:  Dairy Sci Technol       Date:  2013-01-24
  2 in total

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