| pubmed-article:9860181 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9860181 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:9860181 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:9860181 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:9860181 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9860181 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9860181 | pubmed:dateCreated | 1999-3-23 | lld:pubmed |
| pubmed-article:9860181 | pubmed:abstractText | The nature of the proteinaceous film deposited on a biomaterial surface following implantation is a key determinant of the subsequent biological response. To achieve selectivity in the formation of this film, monoclonal antibodies have been coupled to a range of solid substrates using avidin-biotin technology. Antibody clones varied in their antigen-binding activity following insertion of biotin groups into lysine residues. Biotinylated antibodies coupled to solid substrates via an immobilized avidin bridge retained their biological activity. During immobilization of avidin a significant proportion of the protein molecules were passively adsorbed rather than covalently attached to the surface. This loosely bound material could be removed by stringent elution procedures which resulted in a surface density of 5.4 pmol avidin cm(-2). Although these conditions would be harsh enough to denature monoclonal antibodies, they did not destroy the biotin-binding activity of the residual surface-coupled avidin, enabling the subsequent immobilization of biotinylated antibodies. The two-step immobilization technique allowed the use of gentle protein modification procedures, reduced the risk of surface-induced denaturation and removed loosely bound material from the surface. The versatility of the technique encourages its application to a wide range of immobilization systems where retention of biological activity is a key requirement. | lld:pubmed |
| pubmed-article:9860181 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9860181 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860181 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9860181 | pubmed:issn | 0920-5063 | lld:pubmed |
| pubmed-article:9860181 | pubmed:author | pubmed-author:JenkinsMM | lld:pubmed |
| pubmed-article:9860181 | pubmed:author | pubmed-author:SteeleJ GJG | lld:pubmed |
| pubmed-article:9860181 | pubmed:author | pubmed-author:GriesserH JHJ | lld:pubmed |
| pubmed-article:9860181 | pubmed:author | pubmed-author:UnderwoodP... | lld:pubmed |
| pubmed-article:9860181 | pubmed:author | pubmed-author:McFarlandC... | lld:pubmed |
| pubmed-article:9860181 | pubmed:author | pubmed-author:ChatelierR... | lld:pubmed |
| pubmed-article:9860181 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9860181 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:9860181 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9860181 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9860181 | pubmed:pagination | 1207-25 | lld:pubmed |
| pubmed-article:9860181 | pubmed:dateRevised | 2008-2-20 | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
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| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:meshHeading | pubmed-meshheading:9860181-... | lld:pubmed |
| pubmed-article:9860181 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9860181 | pubmed:articleTitle | Albumin-binding surfaces: synthesis and characterization. | lld:pubmed |
| pubmed-article:9860181 | pubmed:affiliation | Cooperative Research Centre for Cardiac Technology, CSIRO Molecular Science, Sydney Laboratory, North Ryde, NSW, Australia. | lld:pubmed |
| pubmed-article:9860181 | pubmed:publicationType | Journal Article | lld:pubmed |
