Linked Life Data

16777063

Source:http://linkedlifedata.com/resource/pubmed/id/16777063

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-6-26
pubmed:abstractText
Potide-G, a small (5578.9 Da) antimicrobial peptide, was isolated from potato tubers (Solanum tuberosum L. cv. Golden Valley) through extraction of the water-soluble fraction, dialysis, ultrafiltration and DEAE-cellulose and C18 reverse-phase high performance liquid chromatography. This antimicrobial peptide was heat-stable and almost completely suppressed the proteolytic activity of trypsin, chymotrypsin and papain, with no hemolytic activity. In addition, potide-G potently inhibited growth of a variety of bacterial (Staphylococcus aureus, Listeria monocytogenes, Escherichia coli, and Clavibacter michiganense subsp. michiganinse) and fungal (Candida albicans and Rhizoctonia solani) strains. Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry revealed that the N-terminal sequence (residues from 1 to 11) of the protein is identical to that of potato proteinase inhibitor, a member of the Kunitz superfamily. And like other members of this class of protease inhibitor, potide-G may have a number of beneficial and therapeutic uses.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
346
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
681-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Purification and characterization of a heat-stable serine protease inhibitor from the tubers of new potato variety "Golden Valley".
pubmed:affiliation
Research Center for Proteineous Materials, Chosun University, Kwangju 501-759, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't