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 in | Biochimica et biophysica acta Vol. 1116; no. 2; pp. 129 - 136 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
22.04.1992
Elsevier |
Subjects | |
Online Access | Get full text |
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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. |
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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 |