Linked Life Data

3604459

Source:http://linkedlifedata.com/resource/pubmed/id/3604459

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1987-8-3
pubmed:abstractText
The peptide fractions isolated from chymotryptic hydrolysates of wheat, rye and barley prolamines [this journal (1984) 178:173] were separated into pure peptides by high-performance liquid chromatography on octadecyl silica gel. The peptides which were most abundant were analyzed for amino acid composition and in part for amino acid sequence. Besides peptides which are typical for only one of the cereals investigated, peptides of similar composition were found in all three prolamines. These contain repeating sequences and are built up of mainly Gln (Q), Pro (P) and hydrophobic amino acids (X) such as Phe, Tyr, Ile, Val and Leu. One of the most frequent partial sequences is QQPQQPXP.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0044-3026
pubmed:author
pubmed:issnType
Print
pubmed:volume
184
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
366-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
[Comparative study of partial amino acid sequences of prolamins and glutelins from various cereals. VII. Amino acid sequences of prolamin peptides].
pubmed:publicationType
Journal Article, Comparative Study, English Abstract, Research Support, Non-U.S. Gov't