Biochemical Studies on Recombinant Human Isobutyryl-CoA Dehydrogenase
Nasser E. Ibrahim1 & Al-Walid A. Mohsen2 Show affiliations
- Minufiya University, Egypt
- University of the Pittsburgh, United States
American Journal of Biochemistry and Biotechnology, Volume 7, Issue 2, pp. 84–89 · doi.org/10.3844/ajbbsp.2011.84.89
Abstract
Problem statement: Human Isobutyryl-CoA Dehydrogenase (IBD) is member of the Acyl-CoA Dehydrogenases family. It is involved in Val metabolism. In this study we modified the purification method of the IBD and further spectroscopic characterization was conducted. Approach: Using DTT in the buffers during the purification, IBD purified to homogeneity by different chromatographic steps. Reactivity of Cys residues were measured using thiol modifying agent DNTB. Results: IBD found to be homotetramer with 42.7 KDa for each subunit and the value of its pI was 6.2. Conclusion: Thiol modifying reagent showed crucial role (s) of some Cys residues for IBD structure, FAD binding and/or activity.
Licence and reuse
Open access. This article is licensed under a Creative Commons Attribution 3.0 Licence (CC BY 3.0), as printed on the article, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original authors and the source. No permission is needed.
How to reuse this articleResponses (0)
About this article
Ibrahim, N. E. & Mohsen, A. A. (2011). Biochemical Studies on Recombinant Human Isobutyryl-CoA Dehydrogenase. American Journal of Biochemistry and Biotechnology, 7(2), 84–89. https://doi.org/10.3844/ajbbsp.2011.84.89
- Licence
- CC BY 3.0
- Issue
- Volume 7, Issue 2
- Policies
- Editorial independenceUse of generative AIData availabilityAppeals and complaints
- Version
- Version of record