ECB-ART-31456
Ukr Biokhim Zh (1978)
1990 Jan 01;624:81-4.
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[Physico-chemical properties of elastase from the sea star Patiria pectinifera].
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An elastolytic protease was purified from the hepatopancreas of the sea star Patiria pectinifera with specific activity of 100 units per 1 mg of protein. The molecular mass of the enzyme was estimated to be 30 KD by SDS-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was shown to be about 7.3 by gel isoelectrofocusing. The pH-dependence of the sea star elastase activity was determined toward Z-Ala-pNA. Values of kKaT and KM were equal to 36 s-1 and 1 mM, respectively. The kinetics of the thermal denaturation of purified elastase was studied at 40 and 60 degrees C. High thermostability and high activity of star elastase permit relying upon successful application of the enzyme in production of different cell cultures.
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Genes referenced: LOC100887844 LOC115919910 LOC594261 LOC752081 LOC756768