Denaturation of Urease Without Inactivation
- 15 October 1948
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 108 (2807) , 410
- https://doi.org/10.1126/science.108.2807.410
Abstract
It has been generally believed that denaturation of an enzyme always coincided with its inactivation. Insoluble urease was prepared from once-recrystallized urease. The material was insoluble in water or dilute phosphate buffer and was highly active, although less so than soluble urease. It gave a strong nitroprusside test for sulfhydryl groups and was much more resistant to digestion by commercial trypsin at pH 7 and 30 C than the same material after boiling. Evidently the reactions which occurred when urease was denatured in this manner did not destroy all of the active groups.Keywords
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