Linked Life Data

15531784

Source:http://linkedlifedata.com/resource/pubmed/id/15531784

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-11-8
pubmed:abstractText
S-layer protein of Bacillus thuringiensis strain CTC was used as the carrier protein to display polyhistidine (poly[6His]) peptides on the cell surface. Poly(6His)n was fused with S-layer protein at two different sites, inserting just downstream of the S-layer protein homologous domain (slh) and replacing the non-slh region of S-layer protein, respectively. The two series chimeric proteins were both expressed by crystal negative B. thuringiensis strain 4Q7 and strain 171, respectively, as shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The recombinant B. thuringiensis cells gained Ni(2+)- and Cd(2+)-binding ability and had a capacity to display up to nine copies of poly(6His). The Cd(2+) adsorption quantity of the recombinant strain with the strongest adsorption ability was twice that of the host strain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0273-2289
pubmed:author
pubmed:issnType
Print
pubmed:volume
119
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-43
pubmed:dateRevised
2008-4-24
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Capacity of Bacillus thuringiensis S-layer protein displaying polyhistidine peptides on the cell surface.
pubmed:affiliation
College of Life Science and Technology, Huazhong Agricultural University, State-Key Laboratory of Agricultural Microbiology, Wuhan 430070, People's Republic of China.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't, Evaluation Studies