Masover G K, Sawyer J E, Hayflick L
J Bacteriol. 1976 Feb;125(2):581-7. doi: 10.1128/jb.125.2.581-587.1976.
The urea-hydrolyzing activity of a T-strain mycoplasma was studied in experiments using whole cells and cell-free enzyme preparations by measuring the release of 14CO2 from [14C]urea. Under the conditions used, the urea concentration optimum is approximately 5.6 X 10(-3) M urea. The activity is soluble and not membrane bound. It is stable at -70 C for several weeks but is more labile at higher temperatures. The pH optimum is between 5.0 and 6.0. The effect of several inhibitors on the activity was tested and revealed similarities, as well as differences, between T-strain mycoplasma urease activity and the urease activity of other organisms and plants.
通过测量[14C]尿素中14CO2的释放量,在使用全细胞和无细胞酶制剂的实验中研究了T株支原体的尿素水解活性。在所使用的条件下,尿素浓度最佳值约为5.6×10(-3)M尿素。该活性是可溶的,不与膜结合。它在-70℃下可稳定数周,但在较高温度下更不稳定。最适pH值在5.0至6.0之间。测试了几种抑制剂对该活性的影响,结果显示T株支原体脲酶活性与其他生物和植物的脲酶活性之间既有相似之处,也有不同之处。