Abstract
We examined the primary structure of α-amylase produced by Bacillus subtilis var. amylosacchariticus by isolation and characterization of CNBr fragments of the enzyme. By solubilization and precipitation in a buffer, the fragments were first fractionated into two. The soluble fraction was fractionated by Bio-Gel P-30, and three fragments were obtained. The insoluble fraction was fractionated by SP-Sephadex C-25 and further purified by Bio-Gels, and five fragments were isolated. Amino acid sequences near the N- and C-terminus were determined with the eight CNBr fragments. By matching the sequences with those of methionine-containing tryptic peptides, alignment of the eight CNBr fragments was determined.
