Purification and Enzymatic Properties of an Endo-α-N-Acetyl-Galactosaminidase from Bacillus laterosporus SS-16

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概要

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• A Gram positive bacterium, Bacillus laterosporus, isolated from soil was found to produce an endo-α-N-acetylgalactosaminidase. The optimum pH of the enzyme was found to be 8.0 and the stable pH range was 3.5-9.0. The apparent K_m values were 0.52 mM and 0.78 mM with asialofetuin and asialo-κ-casein as substrates, respectively. The molecular weight was 210,000 and the isoelectric point was 5.9. The enzyme hydrolyzed the O-glycosidic linkage between α-N-acetylgalactosamine and the hydroxyl group of serine or threonine residues in mucus and mucin-type glycoproteins.

• 公益社団法人日本生物工学会の論文
• 1990-11-25

著者

• Yoshimoto Tadashi

  School Of Pharmaceutical Sciences Nagasaki University

• Tsuru Daisuke

  School Of Pharmaceutical Sciences Nagasaki University

• TAKAHASHI EIJI

  School of Pharmaceutical Sciences, Nagasaki University

• Takahashi Eiji

  School Of Pharmaceutical Sciences Nagasaki University

• Yoshimoto Tadashi

  School of Pharamaceutical Sciences, Nagasaki University

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