Portal de Periódicos da CAPES

Glucose dehydrogenase from Acinetobacter calcoaceticus

1979; Wiley; Volume: 108; Issue: 2 Linguagem: Catalão

10.1016/0014-5793(79)80584-0

1873-3468

J.A. Duine, J. Frank Jzn, J. K. van Zeeland,

Enzyme Catalysis and Immobilization

FEBS LettersVolume 108, Issue 2 p. 443-446 Full-length articleFree Access Glucose dehydrogenase from Acinetobacter calcoaceticus A 'quinoprotein' J.A. Duine, J.A. Duine Laboratory of Biochemistry, Delft University of Technology, 67 Julianalaan 2628 BC Delft, The NetherlandsSearch for more papers by this authorJ.Frank Jzn., J.Frank Jzn. Laboratory of Biochemistry, Delft University of Technology, 67 Julianalaan 2628 BC Delft, The NetherlandsSearch for more papers by this authorJ.K. Van Zeeland, J.K. Van Zeeland Laboratory of Biochemistry, Delft University of Technology, 67 Julianalaan 2628 BC Delft, The NetherlandsSearch for more papers by this author J.A. Duine, J.A. Duine Laboratory of Biochemistry, Delft University of Technology, 67 Julianalaan 2628 BC Delft, The NetherlandsSearch for more papers by this authorJ.Frank Jzn., J.Frank Jzn. Laboratory of Biochemistry, Delft University of Technology, 67 Julianalaan 2628 BC Delft, The NetherlandsSearch for more papers by this authorJ.K. Van Zeeland, J.K. Van Zeeland Laboratory of Biochemistry, Delft University of Technology, 67 Julianalaan 2628 BC Delft, The NetherlandsSearch for more papers by this author First published: December 15, 1979 https://doi.org/10.1016/0014-5793(79)80584-0Citations: 211AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 J.G. Hauge, Methods Enzymol., 9, (1966), 92– 98. 2 J.G. Hauge, J. Biol. Chem., 239, (1964), 3630– 3639. 3 J.A. Duine, J. Frank, J. Westerling, Biochim. Biophys. Acta, 524, (1978), 277– 287. 4 R. De Beer, D. Van Ormondt, M.A. Van Ast, R. Banen, J.A. Duine, J. Frank, J. Chem. Phys., 70, (1979), 4491– 4495. 5 J.A. Duine, J. Frank Jzn, Biochem. J., (1980), in press 6 J. Westerling, J. Frank, J.A. Duine, Biochem. Biophys. Res. Commun., 87, (1979), 719– 724. 7 J.A. Duine, J. Frank Jzn, P.E.J. Verwiel, Eur. J. Biochem., (1980), in press 8 S.A. Salisbury, H.S. Forrest, W.B.T. Crude, O. Kennard, Nature, 280, (1979), 843– 844. 9 W. Olijve, PhD Thesis, (1978), Groningen 10 K. Kersters, J. De Ley, Methods Enzymol., 9, (1966), 346– 354. 11 K. Kersters, J. De Ley, Methods Enzymol., 9, (1966), 170– 179. Citing Literature Volume108, Issue2December 15, 1979Pages 443-446 ReferencesRelatedInformation