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Insulin is an important peptide hormone regulating glucose metabolism. Human insulin consists of two chains (chain-A and chain-B containing 21 and 30 amino acid residues, respectively), two interchain disulphide bonds and one intra disulphide bond within chain-A.
The applicability of capillary zone electrophoresis (CZE) for the separation of the deamidated forms of insulin has been studied. 50 mM NH4Ac (pH=9) with 20 % v/v isopropylalcohol was found optimal for efficient separation of insulin from its even 10 deamidated forms. The developed method was efficiently applied for monitoring the degradation rate of insulin and the formation of different deamidation isoforms.