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Comparison of three phosphorylcholine-binding mouse myeloma proteins by circular dichroism

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/S0006-291X(74)80406-7
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FormatText, Article
Abstract
Circular dichroic spectra of MOPC 167, McPC 603 and TEPC 15 mouse 1gA myeloma proteins in their polymeric and monomeric forms demonstrate that the MOPC 167 protein is quite distinct in structure while the other two show considerable similarity. The differences reside in the Fab portions of the proteins. Binding of phosphorylcholine produced the greatest change in the aromatic region of the spectrum of TEPC 15 monomer and the much more weakly bound hapten, choline, gave virtually the same spectral changes.
Publication date
PublisherElsevier
In
  • Biochemical and Biophysical Research Communications 61, no. 4: 1167–1173.
LanguageEnglish
Peer reviewedYes
NRC numberMORRIS1974
NPARC number9371989
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Record identifierb1d735bf-97e9-4e8b-be4c-0f5266ef4af5
Record created2009-07-10
Record modified2020-03-13
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