Isolation and initial characterisation of complement components C3 and C4 of the nurse shark and the channel catfish.
Complement components C3 and C4 have been isolated from the serum of the nurse shark (Ginglymostoma cirratum) and of the channel catfish (Ictalurus punctatus). As in the higher vertebrates, the fish C4 proteins have three-chain structures while the C3 proteins have two-chain structures. All four proteins have intra-chain thioesters located within their highest molecular mass polypeptides. N-terminal sequence analysis of the polypeptides has confirmed the identity of the proteins. In all cases except the catfish C3 alpha-chain, which appears to have a blocked N-terminus, sequence similarities are apparent in comparisons with the chains of C3 and C4 from higher vertebrates. We have confirmed that the activity/protein previously designated C2n is the nurse shark analogue of mammalian C4. This is the first report of structural evidence for C4 in both the bony and cartilaginous fish.
Dodds
A W
AW
MRC Immunochemistry Unit, University of Oxford, Department of Biochemistry, UK. al@bioch.ox.ac.uk
Smith
S L
SL
Levine
R P
RP
Willis
A C
AC
D000595:Amino Acid Sequence; D000818:Animals; D003176:Complement C3 / Q000737:chemistry* / Q000302:isolation & purification; D003181:Complement C4 / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D007059:Ictaluridae / Q000276:immunology*; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D012754:Sharks / Q000276:immunology*
D003176:Complement C3; D003181:Complement C4