Open AccessPartial amino-acid sequences of human and rabbit C-reactive proteins: homology with immunoglobulins and histocompatibility antigens.
Author(s) -
Alexander P. Osmand,
H Gerwurz,
Bernard Friedenson
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.3.1214
Subject(s) - cyanogen bromide , homology (biology) , peptide sequence , major histocompatibility complex , antibody , antigen , biology , amino acid , histocompatibility , microbiology and biotechnology , biochemistry , chemistry , human leukocyte antigen , genetics , gene
Partial amino-acid sequence analyses of the amino terminus of rabbit C-reactive protein and of a peptide isolated from human C-reactive protein after cyanogen bromide cleavage show an extensive sequence homology between these proteins. Computer analysis detected a distant but significant homology between rabbit C-reactive protein and the CH3 domain of human IgG, In addition, an examination of the limited data available for the amino-acid sequences of human and mouse histocompatibility antigens revealed a similarity between these proteins and C-reactive protein and, therefore, immunoglobulins; These relationships are presented as evidence in support of the hypothesis that C-reactive protein and immunoglobulins share, in addition to functional similarities, a common evolutionary origin with the major histocompatibility antigens.