Linked Life Data

8449956

Source:http://linkedlifedata.com/resource/pubmed/id/8449956

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1993-4-15
pubmed:databankReference
pubmed:abstractText
Of the multiple soluble lactose-binding (S-Lac) lectins in rat intestine, the major one, tentatively designated RI-H, was previously isolated as a polypeptide of molecular weight approximately 17,000. We here report the sequence of RI-H, as determined both at the peptide level and at the nucleotide level. Surprisingly the cDNA encodes a protein of molecular weight approximately 36,000, and this protein contains two homologous but distinct domains each with sequence elements that are conserved among all S-Lac lectins. The C-terminal domain, designated domain II, corresponds to the lectin with M(r) of 17,000 previously isolated from intestinal extracts and shown to have lactose binding activity. By preparing recombinant protein containing only the N-terminal domain, designated domain I, we here directly demonstrate that it too binds lactose and a related range of sugars that are roughly similar to domain II, but clearly distinct. The new lectin, which we designate L-36, is highly expressed in full-length form in rat small and large intestine and stomach but was not detected in eight other tissues including lung, liver, kidney, and spleen. Each domain has approximately 35% sequence identity with the other domain and with the carbohydrate-binding domain of L-29, another S-Lac lectin, but only about 15% identity with other known S-Lac lectins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5929-39
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain.
pubmed:affiliation
Department of Psychiatry, University of California, San Francisco 94143.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't