Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2000-12-1
pubmed:abstractText
The complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat (Fagopyrum esculentum Moench) seeds has been established by automated Edman degradation in combination with MALDI-TOF mass spectrometry. The inhibitor molecule consists of 67 amino acid residues with a single disulfide bond. Its N-terminus is blocked by a pyroglutamic acid residue. The reactive site of the inhibitor contains an Arg43-Asp44 bond. Mass spectrometry revealed that inhibitor BWI-4a is present in buckwheat seeds in two isoforms differing by a single amino acid substitution of Gly40 for Ala40. Analysis of the amino acid sequence of the BWI-4a inhibitor indicates that this inhibitor is a member of the potato proteinase inhibitor I family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2979
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1140-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Complete amino acid sequence of the protease inhibitor BWI-4a from buckwheat seeds.
pubmed:affiliation
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. mbeloz@genebee.msu.su
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't