Studies on the primary structure of .ALPHA.-amylase from Bacillus subtilis var. amylosacchariticus. Part IV. Alignments of tryptic peptides in CNBr fragments of .ALPHA.-amylase from Bacillus subtilis var. amylosacchariticus.

Abstract

To determine the primary structure of the α-amylase produced by Bacillus subtilis var. amylosacchariticus, we have reported the isolation of thirty-four tryptic peptides and eight CNBr fragments from the enzyme. Since the alignment of the eight CNBr fragments was made by matching with six methionine-containing tryptic peptides, the order of tryptic peptides within each CNBr fragment was determined. In the case of four small CNBr fragments, sequence analyses using an automated sequence analyzer established the peptide orders within these fragments. For larger fragments, further fragmentation was done using chymotrypsin or staphylococcal protease V8 and the resultant peptides were isolated and sequenced. Consequently, the peptide orders within three out of four large CNBr fragments were established.