Peculiar effects of temperature and polyvinylalcohol on the activity of bovine serum amine oxidase.

An inflexion point of enzyme activity at 38 - 42 degrees C of the bovine serum amineoxidase was found. This result, associated with non-strict Arrhenius curves and slightly different activation energies in various temperature intervals, suggests some conformational transitions at the mentioned temperatures. The high molecular weight polyvinylalcohol (100,000 Da) generated an activatory effect and a sigmoidal (non-Michaelis) curve of the dependence of the activity on the substrate concentrations, while the low molecular weight polyvinylalcohol (20,000 Da) does not produce this effect. The different ratio of the two types of polyvinylalcohol/enzyme monomer sizes is considered to be responsible for these different effects on the enzyme kinetics.