Proton nuclear magnetic resonance studies of the structure of the Fc fragment of human immunoglobulin G1: Comparisons of native and recombinant proteins

Hironori Matsuda, Satoshi Nakamura, Yataro Ichikawa, Keiji Kozai, Ryo Takano, Masato Nose, Satoshi Endo, Yoshifumi Nishimura, Yoji Arata

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

The structure of the Fc fragment of human IgG1 immunoglobulin is compared for the native and recombinant proteins. A recombinant human Fc fragment was expressed by an E. coli system [Kitai K., Kudo T., Nakamura S., Masegi T., Ichikawa Y. and Horikoshi K. (1988) Appl. Microbiol. Biotechnol. 28, 52-56]. The recombinant protein, which presumably lacks oligosaccharides, was used along with the native human Fc fragment obtained by proteolytic digestion of a myeloma IgG1 protein. 1H NMR has been employed along with circular dichroism and fluorescence spectroscopy to discuss the structure of these two types of proteins. It has been concluded that (1) the overall structure of the recombinant protein is quite similar to that of the native protein, which possesses asparagine-linked oligosaccharides, but (2) a significant difference in structure exists in the neighborhood of the glycosylation site. The difference in the effector functions for the two kinds of the Fc proteins has been briefly discussed in terms of the structural change detected by 1H NMR.

Original languageEnglish
Pages (from-to)571-579
Number of pages9
JournalMolecular Immunology
Volume27
Issue number6
DOIs
Publication statusPublished - 1990 Jun

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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