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Surface characteristics and properties of lumbrokinase-immobilized polyurethane

โœ Scribed by Ryu, Gyu Ha ;Han, Dong Keun ;Park, Seonyang ;Kim, Miran ;Kim, Young Ha ;Min, Byounggoo


Publisher
John Wiley and Sons
Year
1995
Tongue
English
Weight
698 KB
Volume
29
Category
Article
ISSN
0021-9304

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โœฆ Synopsis


Potent and novel fibrinolytic enzymes (lumbrokinase [LK])

were extracted from the earthworm, Lumbricus rubellus.

These enzymes were very stable and showed greater antithrombotic activity than other currently used fibrinolytic proteins. An LK fraction showing the most potent fibrinolytic activity was immobilized onto a polyurethane (PU) surface to investigate its enzymatic activity and antithrombotic activity. A methanol-extracted PU surface was coated with 3% (wt/vol) maleic anhydride methylvinyl ether copolymer (MAMEC)/tetrahydrofuran (THF) solution, and the surface was incubated in an LK solution/phosphatebuffered saline (PBS, pH 7.4). The surface properties were characterized by attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR), electron spectroscopy for chemical analysis (ESCA), and dynamic contact angle. The stability of immobilized LK was determined by caseinolytic activity assay and the specificity of immobilized LK on fibrinogedfibrin was observed by sodium dodecyl


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