Isolation and Alignment of CNBr Fragments of α-Amylase from Bacillus subtilis var. amylosacchariticus
スポンサーリンク
概要
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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.
- 社団法人 日本農芸化学会の論文
著者
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MARUO Bunji
College of Agriculture and Veterinary Medicine, Nihon University
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NAGATA Yoshiho
Division of Enzymology, Institute of Applied Microbiology, The University of Tokyo
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SUGA Shigeto
Division of Enzymology, Institute of Applied Microbiology, The University of Tokyo
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OHKAWA Shuzo
College of Agriculture and Veterinary Medicine, Nihon University
関連論文
- Isolation and Alignment of CNBr Fragments of α-Amylase from Bacillus subtilis var. amylosacchariticus
- Isolation and Amino Acid Sequences of Tryptic Peptides of α-Amylase from Bacillus subtilis var. amylosacchariticus