| Autor: |
Sullivan, C. H., Mather, I. H., Greenwalt, D. E., Madara, P. J. |
| Zdroj: |
Molecular and Cellular Biochemistry; January 1982, Vol. 44 Issue: 1 p13-22, 10p |
| Abstrakt: |
Xanthine oxidase was purified from bovine milk-fat-globule membrane by extraction with butan-1-ol, precipitation with ammonium sulphate, separation by preparative electrofocusing and chromatography on Concanavalin-A/Agarose. The enzyme had an A280/A450 ratio of 4.8 and a specific activity of 3.09. At least five to seven variants of the enzyme with isoelectric points from pH 6.9 to 7.6 were identified. Previously identified minor ‘variants’ of the enzymes with apparently acidic isoelectric points (1) were shown to be the result of aggregation of enzyme with membrane sialoglycoproteins. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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