Abstract:
:The triosephosphate isomerase of Leishmania donovani (LdTIM) was expressed at high level in Escherichia coli. The TIM gene was cloned in expression vector pET-23(a) with C-terminal 6× His tag fused in frame, and expressed as a 27.6-kDa protein in E. coli as inclusion bodies. The recombinant LdTIM from E. coli lysate was solubilized in 6 M guanidine hydrochloride and purified by Ni-NTA chromatography. In the present study, the effect of bovine serum albumin on the reactivation of TIM was investigated. Furthermore, 8-anilino-1-naphthalene sulfonic acid was used to detect the structural changes induced by bovine serum albumin (BSA). Here, we conclude that BSA assists in the refolding and regain of LdTIM enzyme activity by providing framework for structure formation. This study indicates that numerous protein-protein contacts are constantly occurring inside the cell that leads to the formation of native protein.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Kumar K,Bhargava P,Roy Udoi
10.1007/s12010-011-9206-2subject
Has Abstractpub_date
2011-08-01 00:00:00pages
1207-14issue
7eissn
0273-2289issn
1559-0291journal_volume
164pub_type
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