Back to Search
Start Over
Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant
- Source :
- Biochemistry. Jan 5, 1999, Vol. 36 Issue 1, p423, 9 p.
- Publication Year :
- 1999
-
Abstract
- The conformational stability of Plasmodium falciparum triosephosphate isomerase (TIMWT) enzyme was studied in urea and guanidinium chloride (GdmCl) solutions by circular dichroism, fluorescence and size-exclusion chromatography. The dimeric enzyme was observed to be stable in urea solutions. It retained a substantial secondary, tertiary and quaternary structure even in 8 M urea. On the other hand, the unfolding transition was completed by 2.5 M GdmCl.
Details
- ISSN :
- 00062960
- Volume :
- 36
- Issue :
- 1
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.53922027