Linked Life Data

7407235

Source:http://linkedlifedata.com/resource/pubmed/id/7407235

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-11-20
pubmed:abstractText
By affinity chromatography on a concanavalin A-Sepharose column and gel filtration on a Sephadex G-25 column, a glycopeptide of 16 amino acid residues has been separated from a tryptic digest of reduced and carboxymethylated bovine rhodopsin. The glycopeptide was treated with cyanogen bromide and products were subjected to high-voltage paper electrophoresis. N-Blocked homoserine separated was reacted first with anhydrous hydrazine and then with dansyl chloride. The product was identified by thin-layer chromatography to be 1-acetyl-2-dansyl hydrazine, thus showing that the N-terminal blocking group was an acetyl group. The remaining peptide after cyanogen bromide treatment was partially sequenced by the Edman dansylation method. The present results and previously reported findings on the binding site of the sugar moiety, taken together, indicate that the N-terminal heptapeptide has the following structure: acetylMet-Asn(carbohydrate)-Gly-Thr-Glx-Gly-Pro.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
624
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
218-25
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
The N-terminal residue of bovine rhodopsin is acetylmethionine.
pubmed:publicationType
Journal Article