Linked Life Data

8533895

Source:http://linkedlifedata.com/resource/pubmed/id/8533895

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-2-1
pubmed:abstractText
Horseradish peroxidase was activated by periodate oxidation of the carbohydrate moiety and then modified by the covalent attachment of alpha-N,N-bis[carboxyethyl]lysine (CM-Lys) by reductive alkylation using sodium cyanoborohydride. The resultant CM-Lys peroxidase was charged with nickel ions and then used as a specific labeling reagent for histidine-tagged recombinant proteins. This labeling method was effective for proteins that are soluble or insoluble in the absence of chaotropic agents. The labeled proteins were very effective in direct sandwich enzyme-linked immunosorbent assay for detecting antibodies against the protein in sera as demonstrated by assays for antibodies to such diverse viral proteins as hepatitis B surface and core proteins, hepatitis C core and helicase protein (NS3), and retroviral core proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
229
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-60
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Use of alpha-N,N-bis[carboxymethyl]lysine-modified peroxidase in immunoassays.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298-0614, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't