The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus

The amino-acid sequence of a β-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...

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Published inBiochimica et biophysica acta Vol. 1116; no. 2; pp. 129 - 136
Main Authors Muramoto, Koji, Kamiya, Hisao
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 22.04.1992
Elsevier
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Summary:The amino-acid sequence of a β-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 β-galactoside-binding lectin and proved to be a member of the S-type lectin family.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(92)90109-8