The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus.
The amino-acid sequence of a beta-galactoside-binding lectin isolated from the skin mucus of the conger eel Conger myriaster was determined. The lectin (30 kDa) was composed of two identical subunits of 135 amino acid residues with N-acetylserine at the N-terminus and no half-cystinyl residue. It was a 30-34% sequence identical to vertebrate beta-galactoside-binding lectin and proved to be a member of the S-type lectin family.
Muramoto
K
K
School of Fisheries Sciences, Kitasato University, Iwate, Japan.
Kamiya
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003488:Cyanogen Bromide; D004524:Eels; D010450:Endopeptidases; D037161:Galectins; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009092:Mucous Membrane / Q000737:chemistry; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D012867:Skin / Q000737:chemistry*; D014357:Trypsin
D000596:Amino Acids; D037161:Galectins; D037102:Lectins; D010446:Peptide Fragments; C074516:congerin protein, Conger myriaster; D010450:Endopeptidases; D014357:Trypsin; D003488:Cyanogen Bromide