Sequence similarity between alpha 2-macroglobulin from the horseshoe crab, Limulus polyphemus, and proteins of the alpha 2-macroglobulin family from mammals.
1. Purified alpha 2-macroglobulin (alpha 2M) from the American horseshoe crab, Limulus polyphemus was cleaved with trypsin and 20 of the tryptic peptides were sequenced and compared with the sequences of human alpha 2M, rat alpha 1M, alpha 2M, and alpha 1-inhibitor 3, and human complement proteins C3 and C4. 2. Ten of the peptides (233 residues), including that containing the thiol ester site, could be aligned unambiguously with stretches in mammalian alpha 2M, with a degree of identity greater than 30%. 3. The 12-residue thiol ester-containing peptide of Limulus alpha 2M showed 67% identity with the same stretch of human alpha 2M.
Sottrup-Jensen
L
L
Department of Molecular Biology, University of Aarhus, Denmark.
Borth
W
W
Hall
M
M
Quigley
J P
JP
Armstrong
P B
PB
D000595:Amino Acid Sequence; D000818:Animals; D003176:Complement C3; D003181:Complement C4; D006737:Horseshoe Crabs / Q000032:analysis*; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin; D000511:alpha-Macroglobulins
D003176:Complement C3; D003181:Complement C4; D010446:Peptide Fragments; D000511:alpha-Macroglobulins; D014357:Trypsin