Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1980-9-28
pubmed:abstractText
Twelve cyanogen bromide peptides were isolated from S-carboxymethylated mitochondrial aspartate aminotransferase and their amino acid sequences were determined. These peptides were purified first by gel filtration on a Sephadex G-75 column, and then by gel filtration on Bio-Gel, or by ion exchange chromatography on a phosphocellulose column in the presence of 8 M urea, or by both methods. Small peptides were purified by paper chromatography. The cyanogen bromide peptides accounted for 367 of the 401 amino acid residues in the subunit of the enzyme. No peptide accounting for the other 34 residues was obtained in a homogeneous state, but peptide mixtures containing this particular peptide were analyzed by various procedures including Edman degradation and digestion with Staphylococcus aureus protease. The results accounted for all 401 amino acid residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6144-62
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Cyanogen bromide peptides.
pubmed:publicationType
Journal Article