Molecular Weight and Hydrodynamic Properties of a Proteinase A Inhibitor from Baker’s Yeast

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Abstract
The MW of the proteinase A [EC 3.4.23.8] inhibitor IA3 from baker''s yeast was determined by different methods. From gel-filtration experiments, a MW of 19,000 was calculated for the native inhibitor, while under denaturing conditions a MW of 7400 was found. From electrophoretic experiments with the native protein, a MW of 9000 was calculated. A similar value was obtained from the analytical ultracentrifuge, even at a protein concentration of 12 mg/ml. The diffusion coefficient and the partial specific volume were measured and from these data the frictional ratio and the Stokes radius were calculated. These parameters indicate that the relatively high apparent MW calculated from the gel-filtration experiments is caused by the assymetric shape of the inhibitor molecule rather than by an aggregation of subunits.

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