C
C. Roger MacKenzie
Researcher at National Research Council
Publications - 57
Citations - 2684
C. Roger MacKenzie is an academic researcher from National Research Council. The author has contributed to research in topics: Antibody & Single-domain antibody. The author has an hindex of 27, co-authored 54 publications receiving 2530 citations. Previous affiliations of C. Roger MacKenzie include Ontario Agricultural College.
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Journal ArticleDOI
Quantitative Analysis of Bacterial Toxin Affinity and Specificity for Glycolipid Receptors by Surface Plasmon Resonance
TL;DR: In this paper, surface plasmon resonance (SPR) was used for real-time analysis of toxin binding under conditions that mimic the natural cell surface venue of these interactions and without any requirement for labeling of toxin or receptor.
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Pentamerization of Single-domain Antibodies from Phage Libraries: A Novel Strategy for the Rapid Generation of High-avidity Antibody Reagents
Jianbing Zhang,Jamshid Tanha,Tomoko Hirama,Nam Huan Khieu,Rebecca To,Hong Tong-Sevinc,Emily Stone,Jean Robert Brisson,C. Roger MacKenzie +8 more
TL;DR: A novel type of molecule in which single-domain antibodies isolated from a nai;ve llama single domain antibody library are linked to an oligomerization domain to generate high-avidity, antigen-binding reagents that bind strongly to immobilized antigen is described.
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Selection by phage display of llama conventional VH fragments with heavy chain antibody VHH properties
TL;DR: Surprisingly, these V(H) dAbs, which are produced in high yield in Escherichia coli, are highly soluble, have excellent temperature stability profiles and do not display any aggregation tendencies.
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Analysis by Surface Plasmon Resonance of the Influence of Valence on the Ligand Binding Affinity and Kinetics of an Anti-carbohydrate Antibody
C. Roger MacKenzie,Tomoko Hirama,Su-Jun Deng,David R. Bundle,Saran A. Narang,N. Martin Young +5 more
TL;DR: The kinetics of ligand binding by Se155-4, an antibody specific for the Salmonella serogroup B O-polysaccharide, were studied by surface plasmon resonance and indicated that the relatively low affinity of the antibody was due to rapid dissociation.
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Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond
TL;DR: The ds‐scFv form thus combines the stable monomeric form of the disulphide form with the expression advantages of the scFv, and has enhanced thermal stability, by Fourier transform IR spectroscopy.