Research Article Open Access

Biochemical Studies on Recombinant Human Isobutyryl-CoA Dehydrogenase

Nasser E. Ibrahim1 and Al-Walid A. Mohsen2
  • 1 Minufiya University, Egypt
  • 2 University of the Pittsburgh, United States


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.

American Journal of Biochemistry and Biotechnology
Volume 7 No. 2, 2011, 84-89


Submitted On: 27 May 2011 Published On: 12 August 2011

How to Cite: 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.

  • 4 Citations



  • Acyl-CoA dehydrogenase
  • isobutyryl-CoA dehydrogenase
  • valine degradation
  • Sudden Infant Death Syndrome (SIDS)
  • cys residues
  • recombinant human
  • ferricenium assay
  • jamaican vomiting
  • thiol modifying