Abstract
In 1973 Holt and Kinoshita first demonstrated the occurence of a bovine corneal protein with a mass of 54 kDa (BCP 54). This protein has subsequently been shown to be a class 3 aldehyde dehydrogenase which is 84% identical to rat tumor-associated AlDH at the amino acid level (Cooper et al., 1991). Abedinia et al. (1990) purified the bovine corneal AlDH and demonstrated that it was the major soluble protein in bovine cornea, representing 20 to 40% of the soluble protein.
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References
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© 1995 Springer Science+Business Media New York
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Riley, I.K., Burrows, C.A., Hardman, M.J., Buckley, P.D. (1995). Kinetic Studies on Class 3 Aldehyde Dehydrogenase from Bovine Cornea. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_12
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_12
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