Abstract
BECAUSE of the enormously high activity of β-glucuronidase in the preputial gland of the female rat1, this tissue appeared to be a promising source of the purified enzyme. For other tissues employed for this purpose, the specific activity, the degree of purification and the recovery are as follows: ox liver2 (32,000, 800-fold, 5 per cent), calf spleen3 (7,900, 1,400-fold, 1 per cent), calf liver4 (60,000, 9,000-fold, 10 per cent). The specific activity is expressed as µgm. phenolphthalein liberated from phenolphthalein glucuronide by 1 mgm. of protein in 1 hr. at 37° C., and the last two preparations were assayed in presence of deoxyribonucleic acid. A specific activity of 107,000 was observed with the best individual preparation from calf liver4, and this was claimed to represent a purity of 85 per cent.
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LEVVY, G., MARSH, C. Purification of β-Glucuronidase from Female Rat Preputial Gland. Nature 180, 919 (1957). https://doi.org/10.1038/180919a0
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DOI: https://doi.org/10.1038/180919a0
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