Abstract
KB cells, derived from a human nasopharyngeal carcinoma, have high alkaline phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) activity. Specific activity is 150 times higher than in HeLa S3 cells. Alkaline phosphatase activity in KB cells exhibits heterogeneity consisting of a large heat-labile and a small heat-stable component. Enzyme activity is modulated by the osmolality of the culture medium. Increasing the osmolality by the addition of NaCl results in reduction of activity. A similar effect is noted when KB cells are grown with prednisolone (Δ′-hydrocortisone). The activities of acid phosphatase, β-galactosidase and N-acetyl-β-glucosaminidase are not affected by hyperosmolality and/or prednisolone. The reduction in alkaline phosphatase activity is accompanied by an increase in the proportion of the heat-stable and a decrease of the heat-labile enzyme components. The alterations in specific activity and thermostability are independent of the basal culture medium employed. Enzyme stability at 56 °C is inversely related to the buffer concentration, but the differences in stability between the alkaline phosphatases of control cultures and of KB cells grown in hyperosmolar medium or with prednisolone can be recognized with various buffering mixtures.
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