Purification and Properties of Trehalase from Hemolymph of the Pupae of Blowfly, Aldrichina grahami

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概要

• 論文の詳細を見る

• Trehalase (E.C.3.2.1.28) has been isolated from hemolymph of the pupae of blowfly, Aldrichina grahami, and purified approximately 550-fold by chromatography with CM-cellulose, DEAE-cellulose, Sephadex G-150 and ConA-Sepharose. The molecular weight estimated from Sephadex G-200 chromatograpy was 80,000. The enzyme was specific for trehalose. The purified enzyme showed 1.7mM as Km for trehalose, 5.6 for optimum pH and 12.6 kcal/moles as activation energy. The enzyme was inhibited by divalent cation such as Cu^<2+>, Mn^<2+>, Zn^<2+> and Mg^<2+>. The enzyme was inhibited by sucrose, fructose and mannose.

• 大阪府立大学の論文
• 1986-03-31

著者

• Fujii Michiko

  Laboratory Of Biochemistry College Of Agriculture

• Fujii Michiko

  Laboratory Of Applied Molecular Biology College Of Agriculture

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• Purification and Properties of Trehalase from Hemolymph of the Pupae of Blowfly, Aldrichina grahami
• Purification and Properties of Glutamine Synthetase from Germinating Castor Bean Endosperm
• Purification and Properties of Alanine aminotransferase from Germinating Castor Bean Endosperms

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