Abstract
The state of amino acid residues in alkaline protease of Bacillus No. 221 and that of subtilisin BPN' were compared by spectrophotometric titration of tyrosine residues and by several reagents: β-naphtoquinone-4, 6-disulfonic acid and monochlorofluoroquinone for amino groups, H2O2-dioxane for tryptophan, glyoxal for arginine, and tetranitromethane for tyrosine.
The reactivity of both proteases was fairly similar to those reagents.
The helix content of alkaline protease of Bacillus No. 221 (37%) was higher than that of subtilisin BPN' (20%).
The Km and Vmax of alkaline protease of Bacillus No. 221 toward ATEE and BTEE were obtained from Lineweaver-Burk plot and compared with those of α-chymotrypsin and subtilisin BPN'.
