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• W2088897527 abstract "Summary Plasminogen 2 has six glycoforms that differ in their sialic acid content. In this study we have examined the effect that this differential sialylation has on activation of these glycoforms by streptokinase (SK). We find that increases in sialic acid content, above a threshold level, result in a decrease in the catalytic efficiency of activation. This decrease in catalytic efficiency appears to be due to an increase in Km values and a decrease in Kcat values. This phenomenon is most apparent in the activation of plasminogen 2, the most extensively sialyated glycoform with 13 mols of sialic acid/mol protein. Gel filtration demonstrated that SK forms an activator complex with plasminogen 2, indicating that the carbohydrate on plasminogen 2 interferes with the stability of the Michaelis complex, rather than the ability of streptokinase to form activator complexes with plasminogen 2 glycoforms. For comparison we also show data pertaining to activation of plasminogen 2 glycoforms by urinary plasminogen activator and tissue-type plasminogen activator." @default.
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• W2088897527 date "1996-01-01" @default.
• W2088897527 modified "2023-09-24" @default.
• W2088897527 title "The role of carbohydrate in the activation of plasminogen 2 glycoforms by streptokinase" @default.
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• W2088897527 doi "https://doi.org/10.1016/s0268-9499(05)80076-1" @default.
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