rdf:type |
|
lifeskim:mentions |
umls-concept:C0010531,
umls-concept:C0014834,
umls-concept:C0031715,
umls-concept:C0037293,
umls-concept:C0086022,
umls-concept:C0181496,
umls-concept:C0392747,
umls-concept:C0442335,
umls-concept:C0870432,
umls-concept:C1522485,
umls-concept:C1554963,
umls-concept:C1555465,
umls-concept:C1705099,
umls-concept:C1705417
|
pubmed:issue |
2
|
pubmed:dateCreated |
2000-5-4
|
pubmed:abstractText |
We have previously developed the TraT display system to express the preS1 peptide of human hepatitis B virus (HBV) and the snake venom rhodostomin (RHO) on the surface of Escherichia coli. In this study, we modified the pT2 vector by adding a thrombin cutting site and a phosphorylation tag of protein kinase A before the multiple restriction enzyme sites. The modified vector allowed us to label the TraT fusion protein (TraT-RHO) with [32P] and to increase the detection sensitivity of TraT-RHO expression bacteria binding to and being internalized into BHK-21 cells. After the thrombin cleavage, the isotope labeled RHO could be detected in a free form. We therefore suggest that the new version of pT2 vector, pT2-KL, will facilitate to identify the counterpart of displayed peptide.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0168-1656
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
78
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
115-22
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10725535-Amino Acid Sequence,
pubmed-meshheading:10725535-Bacterial Outer Membrane Proteins,
pubmed-meshheading:10725535-Base Sequence,
pubmed-meshheading:10725535-Binding Sites,
pubmed-meshheading:10725535-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:10725535-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10725535-Escherichia coli,
pubmed-meshheading:10725535-Escherichia coli Proteins,
pubmed-meshheading:10725535-Genetic Vectors,
pubmed-meshheading:10725535-Molecular Sequence Data,
pubmed-meshheading:10725535-Peptides,
pubmed-meshheading:10725535-Phosphorus Radioisotopes,
pubmed-meshheading:10725535-Phosphorylation,
pubmed-meshheading:10725535-Recombinant Fusion Proteins,
pubmed-meshheading:10725535-Thrombin
|
pubmed:year |
2000
|
pubmed:articleTitle |
Modification with a phosphorylation tag of PKA in the TraT-based display vector of Escherichia coli.
|
pubmed:affiliation |
Institute of Microbiology, School of Life Science, National Yang-Ming University, Taipei, Taiwan ROC.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|