[Physico-chemical properties of a protein-inhibitor of serine proteinases from the potato].

Serine proteases inhibitor with pl-7.3, isolated from potatoe tubers by isoelectric focusing procedure as described previously (V.V. Mosolov et al., Bioorganic Chem., 1, 1449, 1975), was homogeneous under ultracentrifugation, having sedimentation coefficient S20,w 2.8S. Its molecular weight, investigated by sedimentation equilibrium and gel filtration through Sephadex G-100, was found to be 32500 and 31500 respectively. The Stokes radius R and frictional ratio f/fo were found to be 24 A and 1.14. The molecular weight of the inhibitor as determined by sodium dodecylsulfate polyacrylamide electrophoresis was twice as low as determined in ultracentrifuge and by gel filtration procedure. It is suggested that the inhibitor is dimer and consists of two protomers of equal molecular weight.