Linked Life Data

121997

Source:http://linkedlifedata.com/resource/pubmed/id/121997

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1981-3-24
pubmed:abstractText
Results obtained after digestion of mitochondrial aspartate aminotransferase from pig heart with pepsin and with the protease from S. aureus are described. Peptic digestion produced a very complex mixture of peptides, which were purified and analyzed; structural information contained in these peptides covered nearly the entire molecule. Moreover, the lengths of some individual peptides and the peculiar self-overlapping found with families of peptides from adjacent regions were especially useful and interesting. Not all the possible peptides originating after digestion with S. aureus protease were isolated and examined. However, the high specificity of this protease and its usefulness for sequence studies were confirmed. In particular, the S. aureus peptides obtained were important for establishing the amidation state of glutamic acid/glutamine residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0021-2938
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
478-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage with pepsin and with Staphylococcus aureus protease.
pubmed:publicationType
Journal Article, Comparative Study