Development of a capillary zone electrophoresis method for caseinoglycomacropeptide determination

被引:18
作者
Cherkaoui, S
Doumenc, N
Tachon, P
Neeser, JR
Veuthey, JL
机构
[1] Univ Geneva, Lab Pharmaceut Analyt Chem, CH-1211 Geneva 4, Switzerland
[2] Nestle Res Ctr, CH-1000 Lausanne, Switzerland
关键词
caseinoglycomacropeptide; peptides; validation;
D O I
10.1016/S0021-9673(97)00756-5
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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). (C) 1997 Elsevier Science B.V.
引用
收藏
页码:195 / 205
页数:11
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