TY  - JOUR
AU  - Ibrahim, Nasser E. 
AU  - Mohsen, Al-Walid A. 
PY  - 2011
TI  - Biochemical Studies on Recombinant Human Isobutyryl-CoA Dehydrogenase
JF  - American Journal of Biochemistry and Biotechnology
VL  - 7
IS  - 2
DO  - 10.3844/ajbbsp.2011.84.89
UR  - https://thescipub.com/abstract/ajbbsp.2011.84.89
AB  - 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.