Linked Life Data

2759688

Source:http://linkedlifedata.com/resource/pubmed/id/2759688

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-9-11
pubmed:abstractText
Insoluble complexes of poly-L-histidine (polyhistidine) and catalase were prepared by mixing the two reactants together in solution at pH 5.5 and subsequently elevating the pH to approximately 7.0, at which point they precipitated. Complexes formed at optimal ratios of polyhistidine to catalase contained essentially all of the catalase present in the original solution. The catalase present in such complexes contained greater than 50% of the H2O2-inhibiting activity of the native catalase used to prepare the complexes. The insoluble complexes rapidly bound to viable endothelial cells and were resistant to removal by extensive washing. The presence of polyhistidine-catalase complexes on the cell surface protected the cells against injury mediated by H2O2 or activated polymorphonuclear leukocytes. These data show that polyhistidine-catalase complexes can be prepared that have a high affinity for cells and that retain catalase activity. These complexes may be useful in treating inflammatory conditions in which it is necessary to maintain a high local concentration of inhibitor.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0360-3997
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
465-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Formation and use of poly-L-histidine-catalase complexes: protection of cells from hydrogen peroxide-mediated injury.
pubmed:affiliation
Department of Pathology, University of Michigan Medical School, Ann Arbor 48109.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't