Linked Life Data

6316885

Source:http://linkedlifedata.com/resource/pubmed/id/6316885

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-1-7
pubmed:abstractText
The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues. In conjunction with the amino acid sequence of the 60-residue N-terminal fragment previously determined on the S-peptide released by limited proteolysis with subtilisin the complete sequence of 336 residues was deduced. The sequence has been compared with the 335 residue sequence of pig kidney fructose-bisphosphatase and some areas of sequence for rabbit liver enzyme. The strong homology previously noted for the S-peptide sequence is maintained for the complete enzyme with only 34 changes in 336 residues when comparing the pig and sheep enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0004-9417
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
235-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Amino acid sequence studies on sheep liver fructose-bisphosphatase. II. The complete sequence.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't