Linked Life Data

18601087

Source:http://linkedlifedata.com/resource/pubmed/id/18601087

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2008-7-8
pubmed:abstractText
The chemical adsorption of organic phosphate compounds to alumina has been used to create surface linkers for protein immobilization. A number of particulate alumina supports were screened for their physical properties and ability to bind organic phosphate compounds. Two aluminas, termed C1 and CPC, were selected based on their suitability for subsequent testing as protein immobilization supports. Papain was successfully immobilized to these supports when derivatized with phosphate compounds containing free terminal carboxyl groups. Protein binding was enhanced when support carboxyl groups were activated with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. The level of papain immobilization was dependent upon the length of the linker used and the mass of protein exposed to the support.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3592
pubmed:author
pubmed:copyrightInfo
(c) 1992 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1319-27
pubmed:year
1992
pubmed:articleTitle
Protein immobilization to alumina supports: I. characterization of alumina-organophosphate ligand interactions and use in the attachment of papain.
pubmed:affiliation
Department of Biochemistry, Queen's University, Kingston, Canada.
pubmed:publicationType
Journal Article