Linked Life Data

9095558

Source:http://linkedlifedata.com/resource/pubmed/id/9095558

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-5-13
pubmed:abstractText
Maize C4-type phosphoenolpyruvate carboxylase (PEPC) was expressed in E. coli with the pET32 system. The expressed fusion PEPC was active and its amount comprised more than 10% of total soluble protein. The specific activity increased by about 45-fold, compared with our previous system [S. Yanagisawa and K. Izui, Agric. Biol. Chem., 54, 241-243 (1990)]. The fusion PEPC was rapidly purified with His bind metal chelation resin, showing a single band on SDS-PAGE. Moreover, the tag domain fused at the N-terminus did not have any effect on catalytic and regulatory properties of PEPC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
545-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
High-level expression of maize C4-type phosphoenolpyruvate carboxylase in Escherichia coli and its rapid purification.
pubmed:affiliation
Laboratory of Applied Botany, Faculty of Agriculture, Kyoto University, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't