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  1. Higher-order structure and conformational change in biopharmaceuticals
  2. Robust quantitation of basic-protein higher-order aggregates using size-exclusion chromatography
  3. Understanding the process-induced formation of minor conformational variants of Erwinia chrysanthemi l-asparaginase
  4. Protein deamidation in biopharmaceutical manufacture: understanding, control and impact
  5. Structural Characterisation of Non-Deamidated Acidic Variants of Erwinia chrysanthemi L-asparaginase Using Small-Angle X-ray Scattering and Ion-Mobility Mass Spectrometry
  6. Capillary isoelectric focusing of a difficult-to-denature tetrameric enzyme using alkylurea–urea mixtures
  7. Recombinant Deamidated Mutants of Erwinia chrysanthemi l-Asparaginase Have Similar or Increased Activity Compared to Wild-Type Enzyme
  8. Measurement of Subvisible Particulates in Lyophilised Erwinia chrysanthemi l-asparaginase and Relationship with Clinical Experience
  9. Control of process-induced asparaginyl deamidation during manufacture of Erwinia chrysanthemi l-asparaginase
  10. Validation of a 30-year-old process for the manufacture of l-asparaginase from Erwinia chrysanthemi
  11. Study of radial compression high-performance liquid chromatographic columns for preparative chromatography