Ontology highlight
ABSTRACT: Purpose
Identification of human insulin analogs' impurity with a mass shift +14 Da in comparison to a parent protein.Methods
The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing.Results
The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human insulin and its analogs.Conclusions
Although there are three asparagine residues in the insulin derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.
SUBMITTER: Stadnik D
PROVIDER: S-EPMC6449291 | biostudies-literature | 2019 Apr
REPOSITORIES: biostudies-literature
Stadnik Dorota D Bierczyńska-Krzysik Anna A Zielińska Joanna J Antosik Jarosław J Borowicz Piotr P Bednarek Elżbieta E Bocian Wojciech W Sitkowski Jerzy J Kozerski Lech L
Pharmaceutical research 20190404 6
<h4>Purpose</h4>Identification of human insulin analogs' impurity with a mass shift +14 Da in comparison to a parent protein.<h4>Methods</h4>The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing.<h4>Results</h4>The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human insulin and its ana ...[more]