Abstract
To characterize the calpain inhibitor I-sensitive protease(s) involved in the degradation of HMG-CoA reductase, Simoni’s group (Inoue et al., 1993) attempted to isolate Chinese hamster ovary (CHO) cells resistant to this peptide aldehyde [N-acetyl-leucyl-leucyl-norleucinal (ALLN)]. Instead of inducing a protease, a 35 kDa protein was overexpressed which gave tryptic fragments with a high degree of sequence identity to members of the aldo-ketoreductase superfamily. This superfamily is a rapidly growing group of monomeric oxidoreductases which include the aldehyde and aldose reductases as well as a number of hydroxysteroid dehydrogenases.
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Flynn, T.G., Hyndman, D.J., Takenoshita, R., Vera, N., Pang, S. (1996). Cloning, Sequencing, and Enzymatic Activity of an Inducible Aldo-Keto Reductase from Chinese Hamster Ovary Cells. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_59
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_59
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