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Structural Characterisation of Non-Deamidated Acidic Variants of Erwinia chrysanthemi L-asparaginase Using Small-Angle X-ray Scattering and Ion-Mobility Mass Spectrometry

DOI: 10.1007/s11095-015-1722-2 DOI Help
PMID: 26040662 PMID Help

Authors: David Gervais (Porton Biopharma Limited) , Darryl King (Porton Biopharma Limited) , Patrick Kanda (Porton Biopharma Limited) , Nicholas Foote (Porton Biopharma Limited) , Lucy Elliott (Porton Biopharma Limited) , Phillip Brown (Porton Biopharma Limited) , Natacha O. Lee (University College London) , Konstantinos Thalassinos (University College London) , Claire Pizzey (Diamond Light Source) , Robert Rambo (Diamond Light Source) , Thomas C. Minshull (University of Sheffield) , Mark J. Dickman (University of Sheffield) , Stuart Smith (Porton Biopharma Limited)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Pharmaceutical Research

State: Published (Approved)
Published: June 2015
Diamond Proposal Number(s): 243

Abstract: Erwinia chrysanthemi L-asparaginase (ErA) is an enzyme commonly used in the treatment regimen for Acute Lymphoblastic Leukaemia (ALL). Biopharmaceutical products such as ErA must be monitored for modifications such as deamidation, typically using ion-exchange chromatography (IEX). Analysis of clinical-grade ErA using native IEX resolves a number of enzymatically-active, acidic variants that were poorly characterised.

Subject Areas: Biology and Bio-materials, Medicine


Instruments: B21-High Throughput SAXS