@article{oai:omu.repo.nii.ac.jp:00009339,
 author = {FUJII, Michiko},
 journal = {Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and biology},
 month = {Mar},
 note = {application/pdf, 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., Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and biology. 1986, 38, p.51-59},
 pages = {51--59},
 title = {Purification and Properties of Trehalase from Hemolymph of the Pupae of Blowfly, Aldrichina grahami},
 volume = {38},
 year = {1986}
}