Literature DB >> 12240950

Characterization of asparagine deamidation and aspartate isomerization in recombinant human interleukin-11.

Wei Zhang1, J Marta J Czupryn, Philip T Boyle, John Amari.   

Abstract

UNLABELLED: PURPOSE; The aim of this study was to investigate asparagine (Asn) deamidation and aspartate (Asp) isomerization and to measure the content of isoaspartate (isoAsp) in recombinant human interleukin-11 (rhIL-11).
METHODS: The rhIL-11 control and heat stressed samples were characterized with trypsin and endoproteinase Asp-N peptide mapping, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), reversed-phase high performance liquid chromatography (RP-HPLC), electrospray ionization mass spectrometry (ESI MS) and capillary electrophoresis (CE). The total isoAsp content and bioactivity were also assessed.
RESULTS: Stress of rhIL11 at 30 degrees C for 6 weeks in liquid resulted in significant isomerization of Asp45 and Asp47. Isomerization of Asp51 and deamidation of Asn49 were also detected at low levels. The stressed rhIL-11 molecule contained 0.3 mol of isoAsp per mol of protein, compared to only 0.007 mol/mol of protein in the control.
CONCLUSIONS: Asp and Asn residues, located in a loop structure of rhIL-11, undergo isoAsp formation under stressed conditions.

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Year:  2002        PMID: 12240950     DOI: 10.1023/a:1019814713428

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


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