Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-10-18
pubmed:abstractText
The complete amino acid sequence of SJL-I, a lectin from the sea cucumber, Stichopus japonicus, was determined by sequence analysis of peptides derived on enzymatic and chemical fragmentation of the protein. SJL-I consists of 143 amino acid residues and its molecular mass was calculated to be 15,837 Da. Comparison of the sequence of SJL-I with a database revealed that SJL-I exhibits apparent homology with C-type lectins, especially with those of marine invertebrates. The highest homology (identity 28.6%) was found with echinoidin, a lectin from the sea urchin, Anthocidaris crassispina. Comparison of the sequence of SJL-I with those of other C-type lectins indicated that the conserved amino acids are relatively abundant in the C-terminal half of their carbohydrate-recognition domains (CRDs), that can be considered to be involved in binding with Ca2+ as well as carbohydrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
689-92
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Amino acid sequence of a lectin from the sea cucumber, Stichopus japonicus, and its structural relationship to the C-type animal lectin family.
pubmed:affiliation
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't