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The Role of Sialic Acid in the Determination of Distinct Properties of the Isozymes of Rabbit Plasminogen

From the ¹ From the Department of Chemistry, Program in Biochemistry and Biophysics, The University of Notre Dame, Notre Dame, Indiana 46556

Previous studies from our laboratory have resulted in the separation of two major forms of plasminogen from rabbit plasma. These two forms differ in their affinity characteristics for antifibrinolytic amino acids, metabolic survival times in the circulation, charge characteristics of the subforms resolved from each major form, and sialic acid content. In order to investigate the role of sialic acid in determining these distinct properties of the plasminogen forms, we have studied these same properties of the asialo rabbit plasminogen forms. We find that the charge differences between the two forms are essentially abolished upon removal of the sialic acid. The number of subforms resolved from each major form is decreased as an effect of removal of the sialic acid, but the remaining subforms possess greatly increased isoelectric points. Contrarily, the binding of each plasminogen to antifibrinolytic amino acids appears no different from normal. The metabolic survival times of the asialoplasminogen forms are not greatly different from each other but are significantly lower than normal, a phenomena also found for many other circulating proteins. These studies suggest that the charge differences between the two forms of rabbit plasminogen are incidental to their functional differences.

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