Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-10-12
pubmed:abstractText
The Trypanosoma brucei and Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenases have been overexpressed in Escherichia coli using a T7 expression system. These enzymes have been highly purified by ammonium sulfate precipitation, followed by phenyl-Sepharose and phospho-ultrogel chromatography. From 1 liter of bacterial culture, we obtained 4.4 mg of T. brucei enzyme, with a specific activity of 147 units/mg, and 26.6 mg of T. cruzi enzyme, with a specific activity of 122 units/mg. Both proteins have a similar subunit mass of 38 kDa. Some physicochemical and kinetic properties have been determined and compared with those reported for the authentic T. brucei enzyme. The two enzymes appear to be very similar, except for the dependence of their activity on ionic strength.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1046-5928
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
244-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Glycosomal glyceraldehyde-3-phosphate dehydrogenase of Trypanosoma brucei and Trypanosoma cruzi: expression in Escherichia coli, purification, and characterization of the enzymes.
pubmed:affiliation
Research Unit for Tropical Diseases, International Institute of Cellular and Molecular Pathology, Brussels, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't