Abstract
Purpose: to investigate the dependence of the thrombolytic activity of tissue plasminogen activators (tPA) alteplase and tenecteplase on the degree of sialylation of the oligosaccharide component of molecules. Materials and methods: tPA specimens with an average degree of sialylation were obtained by cultivating CHO clones-producers in the fed-batch mode; desialylated forms of tPA were obtained by processing with neuraminidase, and hypersialylated forms of tPA were obtained by cultivating clones-producers in a medium with the addition of butyrate. The content of sialic acids was determined by resorcinol method, and the activity of tPA was determined by fibrin clot lysis. Results: the dependence of tenecteplase activity on the content of sialic acids in the molecule is demonstrated. The activity of tenecteplase falls below the limits of the target range when the content of sialic acids is more than 5 residues per tenecteplase molecule. No such relation was found for alteplase. Conclusion: the content of sialic acid residues affects the biological activity of tenecteplase; the activity of alteplase does not depend on the degree of sialylation of the molecule.
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