Abstract
In the preceeding paper, purification procedure and some enzymatic properties of thiaminase 11 produced intracellularly from Bacillus aneurinolyticus were reported. In this paper the physicochemical properties of the enzyme was de-scribed. Thiaminase 11 had a molecular weight of 180,000 determined by gel filtration. The physicochemical values of the enzyme protein were 5.88 (S^0_<20.w.>), 0.792 cm^3/g (sp. vol.), 2.89×10^<-7>cm/sec of (diffusion const.) and 182,000 (mol. wt.) calculated from these constants supporting the result of gel filtration. The enzyme consisted of 10 homogeneous polypeptides and the subunit was composed of 175 amino acids including three SH groups. The enzyme contained one mole of glucosamine per subunit and some sugars, indicating that the enzyme is a glycoprotein. The amino-terminal amino acid was Met and carboxy-terminal Ser. Isoelectric point of the enzyme was 4.55.
