タカアミラ-ゼAの全一次構造 (アミラ-ゼシンポジウム(1982)特集〔含 討論〕)
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概要
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Taka-amylase A (TAA) [EC 3.2.1.1 α-1, 4-glucan 4-glucanohydrolase, Aspergillus oryzae], which crystallized first by S. Akabori et al, in 1951, is a glycoprotein consisting of a single polypeptide chain of 478 amino acid residues with an amino-terminal alanine and a carboxylterminal serine. Crystalline TAA was further purified by ion-exchange chromatography on a DEAE-cellulose column. The homogeneous enzyme judged by polyacrylamide gel electrophoresis was reduced and carboxymethylated. The cyanogen bromide cleavage at methionine residues of the reduced and carboxymethylated TAA (RCM-TAA) was performed in 70% formic acid for 24 hr at room temperature. TAA contains nine methionine residues and the following ten CNBr fragments were isolated; CN 1(1-55), CN 2(56-112), CN3(113-115), CN4(116-123), CN5(124-246), CN6(247-269), CN 7(270-275), CN 8(276-395), CN 9(396-454) and CN 10(455-478). Their amino acid sequences were determined by automated Edman degradation or by the manual Edman method. Methionine-containing peptides were isolated from tryptic and chymotryptic digests of the maleylated RCM-TAA. The alignment of the CNBr fragments were performed based on the amino acid sequences of methionine-containing peptides and the entire amino acid sequence of TAA was established. The N-terminal sequences of α-amylases from various origins were compared. No sequence similarity among TAA, bacterial and animal α-amylases was found in their N-terminal regions. When the amino acid sequence of TAA was compared with those of animal (mouse, rat and hog) a-amylases, sequence homologies between TAA and animal α-amylases and among mouse, rat and hog were about 24% and 77%, respectively. Furthermore, on the view point of the structure and function relationship, some possibilities of a few residues as active sites in α-amylase were discussed.
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