Hemerythrin from Lingula unguis consists of two different subunits, alpha and beta.
Hemerythrin, a non-heme Fe-protein, of Lingula unguis has an octamer structure. We demonstrated that the protein is composed of two distinct subunits (alpha and beta), in equal amounts by investigation of their composition and partial terminal sequence. The cross-linking reaction of the native protein with dithiobis-(succinimidyl propionate) provided evidence for the presence of a dimer composed of alpha and beta subunits.
Satake
K
K
Department of Chemistry, Faculty of Science, Science University of Tokyo, Japan.
Yugi
M
M
Kamo
M
M
Kihara
H
H
Tsugita
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006422:Hemerythrin / Q000032:analysis; D007448:Invertebrates / Q000235:genetics*; D046911:Macromolecular Substances; D008667:Metalloproteins / Q000032:analysis; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013388:Succinimides / Q000494:pharmacology
D000596:Amino Acids; D003432:Cross-Linking Reagents; D006422:Hemerythrin; D046911:Macromolecular Substances; D008667:Metalloproteins; D013388:Succinimides; C011240:dithiobis(succinimidylpropionate)