Studies on the properties of immobilized urokinase: effects of pH and temperature

Human urokinase was immobilized on an ethylene vinyl acetate copolymer surface. Soluble urokinase showed its maximum activity at pH 8.5, while the immobilized enzyme was most active at pH 9.0. Apparently, the shift in optimal pH was due to the polyanionic nature of the carrier surface on which the e...

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Bibliographic Details
Published inBiotechnology and applied biochemistry Vol. 10; no. 3; p. 294
Main Author Yabushita, Y
Format Journal Article
LanguageEnglish
Published United States 01.06.1988
Subjects
Enzyme Stability
Enzymes, Immobilized - analysis
Hot Temperature
Humans
Hydrogen-Ion Concentration
Urokinase-Type Plasminogen Activator - analysis
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Summary:Human urokinase was immobilized on an ethylene vinyl acetate copolymer surface. Soluble urokinase showed its maximum activity at pH 8.5, while the immobilized enzyme was most active at pH 9.0. Apparently, the shift in optimal pH was due to the polyanionic nature of the carrier surface on which the enzyme was immobilized. Optimal temperatures of soluble urokinase and immobilized enzyme were identical, i.e., 37 degrees C. The stability of immobilized enzyme against thermal degradation was several times higher than that of the soluble enzyme. Its stability at higher temperatures is one of the main reasons for the clinical use of immobilized urokinase as an antithrombotic material.
ISSN:0885-4513
1470-8744
DOI:10.1111/j.1470-8744.1988.tb00020.x