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- W2315691245 abstract "Neuraminidase in platelets was puified by colominic acid starch gel affinity chromatography.Platelets in 0.01% triton X-100 of 1/5 vol. ACD-saline were sonicated by 50W for 2min at 5°C and fractioned with saturated ammonium sulfate. Neuraminidase in the fraction was purified by affinity chromatography. The highest concentration of neuraminidase was obtained with 20ml of 100mM acetate buffer, pH 5.0. The specific activity of the neuraminidase was 9.030u/mg when the fraction was ultrafiltrated, though other trace amount of enzymes such as galactosidase, glucosidase and mannosidase were found.The study on neuraminidase in platets revealed the following. By using SDS-PAGE, two bands wends found indicating moleculecular weights of 82000 and 69000. The activity of neuraminidase in the platelets was approximately 10-3 units/108 p latelets. The optimum pH's for enzyme activity in neuraminidase were 4.2 when colominic acid substrate was used and 3.0 or less when NANA-4MU was used. The values of Km in NANA-lactose were 2.0×10-5M, 4.0×10-4M and 1.6×10-5M for fetuin, colominic acid and NANA-4MU substrates respectively.The study also indicated that neuraminidase appeared to adhere firmly to the platelet membrane." @default.
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- W2315691245 date "1985-01-01" @default.
- W2315691245 modified "2023-10-03" @default.
- W2315691245 title "Characterization and purification of neuraminidase in human platelet." @default.
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- W2315691245 doi "https://doi.org/10.2491/jjsth1970.16.68" @default.
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