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Effect of sodium thiomalate on immune complex-induced release of lysosomal enzymes from human polymorphonuclear
The extracellular release of beta-glucuronidase and beta-N-acetylglucosaminidase from normal human polymorphonuclear leucocytes initiated with bovine serum albumin/anti-bovine serum albumin immune complex (15 micrograms/ml) was significantly inhibited (p less than 0.01) by pretreatment with increasing concentrations (10(-8) M, 10(-7) M, 10(-6) M and 10(-5) M) of sodium thiomalate in a time- and dose-related fashion. Also, beta-glucuronidase and beta-N-acetylglucosaminidase exhibited similar responses to the effects of bovine serum albumin/anti-bovine serum albumin or sodium thiomalate. In contrast, neither bovine serum albumin/anti-bovine serum albumin nor sodium thiomalate provoked appreciable leakage of the cytoplasmic enzyme, lactate dehydrogenase. This indicates that cell integrity remains intact under the experimental conditions described.
The extracellular release of beta-glucuronidase and beta-N-acetylglucosaminidase from normal human polymorphonuclear leucocytes initiated with bovine serum albumin/anti-bovine serum albumin immune complex (15 micrograms/ml) was significantly inhibited (p less than 0.01) by pretreatment with increasing concentrations (10(-8) M, 10(-7) M, 10(-6) M and 10(-5) M) of sodium thiomalate in a time- and dose-related fashion. Also, beta-glucuronidase and beta-N-acetylglucosaminidase exhibited similar responses to the effects of bovine serum albumin/anti-bovine serum albumin or sodium thiomalate. In contrast, neither bovine serum albumin/anti-bovine serum albumin nor sodium thiomalate provoked appreciable leakage of the cytoplasmic enzyme, lactate dehydrogenase. This indicates that cell integrity remains intact under the experimental conditions described.