Substitution of asparagine324 with aspartic acid in the fc portion of mouse antibodies reduces their capacity for clq binding

Masato Nose, Thomas Leanderson

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

The sequence of the heavy chain C region of mouse mutant IgG2a antibodies with reduced capacity for Clq binding but with retained ability for Fc receptor‐mediated functions was determined by cDNA cloning and by mRNA sequencing. The specific mutation was found to be the substitution of asparagine324 with aspartic acid. Asparagine324 represents a new residue relating to the Clq‐binding sites previously described.

Original languageEnglish
Pages (from-to)2179-2181
Number of pages3
JournalEuropean Journal of Immunology
Volume19
Issue number11
DOIs
Publication statusPublished - 1989 Nov

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint Dive into the research topics of 'Substitution of asparagine<sup>324</sup> with aspartic acid in the fc portion of mouse antibodies reduces their capacity for clq binding'. Together they form a unique fingerprint.

Cite this