An active monomeric form of bovine milk xanthine oxidase
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Upon gel filtration, the commercial bovine milk xanthine oxidase preparation was fractionated into two preparations showing enzyme activity. Native polyacrylamide gel electrophoresis showed that one was in a dimeric form and the other was a monomer having molecular weight of 150 kDa. It was also found that this commercial enzyme existed mostly in an active monomeric form without loss of enzyme activity. The rabbit antisera produced against two enzyme preparations cross-reacted well each other. In SDS-polyacrylamide gel electrophoresis, however, both enzyme preparations yielded two smaller protein bands below 150 kDa, which appeared to bind with both antisera with high affinity but not to retain enzyme activity. It implies that bovine milk xanthine oxidase can lose its activity when monomeric subunit is further degraded.
Key wordsBovine milk xanthine oxidase Active monomeric subunit
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- Parks, D. A. and Granger, D. N., Xanthine oxidase: biochemistry, distribution and physiology.Acta Phys. Scand., 548, 87–99 (1986).Google Scholar