Linked Life Data

16601766

Source:http://linkedlifedata.com/resource/pubmed/id/16601766

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-4-7
pubmed:abstractText
The aim of this work was isolation and purification of the major immunodominant protein, Outer surface protein C (OspC) of three members of the species group Borrelia burgdorferi, the causative agent of Lyme disease. Our aim was to obtain this protein in a quantity and purity sufficient for immunization of experimental animals. For optimalization of protein purification's yield we used immobilized metal ion affinity chromatography (IMAC) under different conditions. The greatest efficiency was achieved by using of HiTrap Chelating Column under native conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1213-8118
pubmed:author
pubmed:issnType
Print
pubmed:volume
149
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
261-4
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Isolation and purification of recombinant outer surface protein C (rOspC) of Borrelia burgdorferi sensu lato.
pubmed:affiliation
Department of Immunology, Palacký University, Olomouc, Czech Republic. majkl.krupka@centrum.cz
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't