Linked Life Data

17936696

Source:http://linkedlifedata.com/resource/pubmed/id/17936696

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2007-11-26
pubmed:databankReference
pubmed:abstractText
An anionic peroxidase from sweetpotato tubers is purified and characterized. The isozyme ibPrx15 is purified to homogeneity by affinity chromatography using a concanavalin A column. The isoelectric point was determined to pI 4.9. MALDI-MS detected a singly charged molecule with a mass of 42029 Da. Absorption spectra of ibPrx15 compounds I, II and III were obtained after treatment with H(2)O(2) at room temperature. Comparative data of ibPrx15 on substrate specificity to tobacco anionic peroxidase (TOP) and horseradish peroxidase (HRP) reveal similar specific activity towards a series of conventional substrates except for iodide, which is a two-electron donor interacting directly with the compound I derivative in the catalytic cycle. ibPrx15 exhibits a high specific activity towards iodide about 10(3)-fold to that of tobacco peroxidase. The amino acid sequence of the main isozyme ibPrx15 was determined by Edman degradation and by sequencing the amplified cDNA fragments. ibPrx15 has 86% identity to another Ipomoea sequence ibPrx05 and 72% identity with a sequence from Populus trichocarpa (PtPrx72).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1774
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1422-30
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Purification, cloning and characterization of a novel peroxidase isozyme from sweetpotatoes (Ipomoea batatas).
pubmed:affiliation
Institut für Biochemie, Westfälische Wilhelms-Universität, Wilhelm-Klemm-Strasse 2, D-48149 Münster, Germany. romela@uni-muenster.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't