Study of an intracellular α‐galactosidase from the thermophilic fungus penicillium duponti
1976; Wiley; Volume: 18; Issue: 4 Linguagem: Inglês
10.1002/bit.260180409
ISSN1097-0290
AutoresNicole Arnaud, David A. Bush, M. Horisberger,
Tópico(s)Enzyme Catalysis and Immobilization
ResumoBiotechnology and BioengineeringVolume 18, Issue 4 p. 581-585 Communications to the EditorFree Access Study of an intracellular α-galactosidase from the thermophilic fungus penicillium duponti Nicole Arnaud, Nicole Arnaud Research Department, Nestlé Products Technical Assistance Co. Ltd., Ch-1814 La Tour-de-Peilz, SwitzerlandSearch for more papers by this authorDavid A. Bush, David A. Bush Research Department, Nestlé Products Technical Assistance Co. Ltd., Ch-1814 La Tour-de-Peilz, SwitzerlandSearch for more papers by this authorMarc Horisberger, Marc Horisberger Research Department, Nestlé Products Technical Assistance Co. Ltd., Ch-1814 La Tour-de-Peilz, SwitzerlandSearch for more papers by this author Nicole Arnaud, Nicole Arnaud Research Department, Nestlé Products Technical Assistance Co. Ltd., Ch-1814 La Tour-de-Peilz, SwitzerlandSearch for more papers by this authorDavid A. Bush, David A. Bush Research Department, Nestlé Products Technical Assistance Co. Ltd., Ch-1814 La Tour-de-Peilz, SwitzerlandSearch for more papers by this authorMarc Horisberger, Marc Horisberger Research Department, Nestlé Products Technical Assistance Co. Ltd., Ch-1814 La Tour-de-Peilz, SwitzerlandSearch for more papers by this author First published: April 1976 https://doi.org/10.1002/bit.260180409Citations: 12AboutPDF 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 P. M. Dey and J. P. Pridham, Advan. in Enzymol., 36, 91 (1972). 2 N. Nelson, J. Biol. Chem., 153, 375 (1944). 3 O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem., 193, 265 (1951). 4 I. Croon and R. St. J. Manley, Meth. Carbohydr. Chem., 3, 280 (1963). 5 K. Weber and M. Osborn, J. Biol. Chem., 244, 4406 (1969). 6 O. P. Bahl and K. M. L. Agrawal, J. Biol. Chem., 244, 2970 (1969). 7 Y.-T. Li and M. R. Shetlar, Arch. Biochem. Biophys., 108, 523 (1964). 8 H. Suzuki, S.-C. Li, and Y.-T. Li, J. Biol. Chem., 245, 781 (1970). 9 Y.-T. Li, S.-C. Li, and M. R. Shetlar, Arch. Biochem. Biophys., 103, 436 (1963). 10 H. Sugimoto and J. P. Van Buren, J. Fd. Sci., 35, 655 (1970). 11 H. Suzuki, Y. Ozawa, and O. Tanabe, Agr. Biol. Chem., 30, 1039 (1966). 12 J. Delente and K. Ladenburg, J. Fd. Sci., 37, 372 (1972). Citing Literature Volume18, Issue4April 1976Pages 581-585 ReferencesRelatedInformation
Referência(s)