Isolation and Amino Acid Sequences of Tryptic Peptides of α-Amylase from Bacillus subtilis var. amylosacchariticus

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概要

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• We examined the primary structure of the α-amylase produced by Bacillus subtilis var. amylosacchariticus by attempting to isolate tryptic peptides of the enzyme. By solubilization and precipitation in buffers, the peptides were first fractionated into three. The main fraction was fractionated by ion-exchange chromatography. Twenty-seven peptides were generated from this fraction. The fraction insoluble at neutral pH was fractionated by SP-Sephadex C-25. From this fraction three peptides were obtained. The other fraction insoluble at acidic pH was fractionated by Bio-Gel P-60. Four peptides were isolated from this fraction. In total, thirty-four peptides were generated from the tryptic digest of the α-amylase. The amino acid sequences of twenty-one out of thirty-four peptides were completely determined, while those of the other thirteen peptides were partially determined. The peptides derived from the N- and C-terminal ends of the α-amylase were identified.

• 社団法人 日本農芸化学会の論文

著者

• MARUO Bunji

  College of Agriculture and Veterinary Medicine, Nihon University

• NAGATA Yoshiho

  Division of Enzymology, Institute of Applied Microbiology, The University of Tokyo

• SUGA Shigeto

  Division of Enzymology, Institute of Applied Microbiology, The University of Tokyo

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

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