PMID: 2500969Apr 18, 1989Paper

Comparison of the Fc fragment from a human IgG1 and its CH2, pFc', and tFc' subfragments. A study using reductive methylation and 13C NMR

Biochemistry
J E Jentoft, R Rayford

Abstract

The Fc fragment of a human monoclonal IgG1 was compared with subfragments containing (a) the intact CH2 domain (CH2 fragment) or (b) the intact CH3 domain (pFc' and tFc' fragments). All fragments were reductively 13C-methylated and their resulting dimethyllysyl resonances characterized in 0.1 M KC1 as a function of pH by 13C NMR spectroscopy. Seven resonances were characterized for the 18 lysine residues of the Fc fragment, eight for the 12 lysines of the CH2 fragment, and five each for the 18 lysine residues of the Fc fragment, eight for the 12 lysines of the CH2 fragment, and five each for the 9 lysines of the pFc' and the 6 lysines of the tFc' fragments, respectively. The multiplicity of resonances indicates that the lysine residues in each fragment exist in a variety of microenvironments and that the fragments are all highly structured. The correspondence between 6 of the 12 or 13 perturbed lysine residues in the Fc fragment and the smaller subfragments indicates that the conformation of the CH2 and CH3 domains is largely unchanged in the smaller fragments. However, in addition to three lysines at the CH2-CH3 domain interface, whose environments were known to be disrupted in the smaller fragments, three or four lysine resid...Continue Reading

References

May 1, 1969·Proceedings of the National Academy of Sciences of the United States of America·G M EdelmanM J Waxdal
Feb 14, 1971·Journal of Molecular Biology·B Lee, F M Richards

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Citations

Dec 17, 1998·Trends in Cell Biology·P EggletonA J Tenner
Dec 1, 1993·Journal of Protein Chemistry·M E Huque, H J Vogel
Jun 30, 2006·Colloids and Surfaces. B, Biointerfaces·Haiying TangK Y Simon Ng
Jul 4, 2002·Journal of the American Chemical Society·Kristi J HumphreysSteven E Rokita
Jun 26, 2007·Inorganic Chemistry·Arturo RobertazziJan Reedijk

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