Effects of Unsaturated Uronic Acid Residues at Non-reducing End on Bond Cleavage Frequency of Poly(1, 4-α-L-guluronide) Lyase from Enterobacter cloacae M-1
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概要
- 論文の詳細を見る
The mode of attion of poly(1, 4-α-guluronide) lyase from Enterobacter cloacae M-1 on unsaturated oligoguluronic acids was studied using fluorophore-assisted carbohydrate electrophoresis. The polyguluronate lyase degraded unsaturated penta-, hexa-, and heptaguluronic acids, but not unsaturated oligoguluronic acids with DPs less than 4. On comparison with the aspect of enzymatic degradation of unsaturated oligoguluronic acid and saturated oligoguluronic acid having the same DP, the former was degraded faster than the latter, and also the cleavage pattern of the polyguluronate lyase on unsaturated oligoguluronic acids was considerably different from that on saturated oligoguluronic acids. From the results described above, we suggest that the affinity of the first subsite from the non-reducing end side of the enzyme to Δ residues is lower than that to GulA residues.
- 社団法人日本農芸化学会の論文
- 1998-01-23
著者
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Kusakabe Isao
Institute of Applied Biochemistry, University of Tsukuba
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YOSHIDA Shigeki
Institute of Applied Biochemistry, University of Tsukuba
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SHIMOKAWA Tomoko
Institute of Applied Biochemistry, University of Tsukuba
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Yoshida S
Plant Science Center Riken Institute
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Yoshida S
Cancer Immunotherapy Center Nagoya Kyoritu Hospital
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Yoshida S
Laboratory Of Cancer Cell Biology Research Institute For Disease Mechanism And Control Nagoya Univer
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Yoshida Shigeki
Inst. Applied Biochem. Tsukuba Univ.
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SHIMOKAWA Tomoko
Forestry and Forest Products Res. Inst.
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Kusakabe I
Univ. Tsukuba Tsukuba Jpn
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Kusakabe Isao
Institute Of Applied Biochemistry University Of Tsukuba
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Yoshida Shigeki
Institute Of Applied Biochemistry University Of Tsukuba
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