@article {10.3844/ajbbsp.2011.84.89,
article_type = {journal},
title = {Biochemical Studies on Recombinant Human Isobutyryl-CoA Dehydrogenase},
author = {Ibrahim, Nasser E. and Mohsen, Al-Walid A.},
volume = {7},
number = {2},
year = {2011},
month = {Aug},
pages = {84-89},
doi = {10.3844/ajbbsp.2011.84.89},
url = {https://thescipub.com/abstract/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.},
journal = {American Journal of Biochemistry and Biotechnology},
publisher = {Science Publications}
}