Linked Life Data

15707684

Source:http://linkedlifedata.com/resource/pubmed/id/15707684

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-2-14
pubmed:abstractText
Chimeric proteins combining the catalytic N-terminal region of native EngD with its proline-threonine-threonine (PT) linker region, hydrophilic domain (HLD) and cellulose binding domain (CBD) of cellulose binding protein A (CbpA) from Clostridium cellulovorans were constructed, expressed, and analyzed. The chimeric proteins with CBD(CbpA) all demonstrated strong affinity to Avicel. The chimeric protein with the PT region of EngD and the HLD had the best catalytic activity and the highest estimated percentage of soluble protein amongst the chimeric proteins. Native EngD and two of the chimeric proteins (EngD-PT-HLD-CBD and EngD-CBD) were purified and their characteristics analyzed. Their binding affinities to Avicel as well as their enzymatic activities against various substrates were found to be consistent with the results we saw from protein lysate samples, which was good binding to Avicel but a decrease in solubility and catalytic activities in chimeric proteins without PT and/or HLD. The reasons for these are discussed. These fusion proteins may be important in applications, such as immobilization to solid cellulose substrate for purification of proteins and enrichment/aggregation of protein complexes.
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
30
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
233-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Effects of the PT region of EngD and HLD of CbpA on solubility, catalytic activity and purification characteristics of EngD-CBD(CbpA) fusions from Clostridium cellulovorans.
pubmed:affiliation
School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't