The purification and properties of an aryl [beta]-hexosidase from bovine liver
dc.contributor.author | Distler, Jack J. | en_US |
dc.contributor.author | Jourdian, George W. | en_US |
dc.date.accessioned | 2006-04-07T17:13:35Z | |
dc.date.available | 2006-04-07T17:13:35Z | |
dc.date.issued | 1977-01-30 | en_US |
dc.identifier.citation | Distler, Jack J., Jourdian, George W. (1977/01/30)."The purification and properties of an aryl [beta]-hexosidase from bovine liver." Archives of Biochemistry and Biophysics 178(2): 631-643. <http://hdl.handle.net/2027.42/22995> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DYM9J4-1MY/2/6f07a2e85e9a2d971bd0fb92a714694d | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22995 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13736&dopt=citation | en_US |
dc.description.abstract | An aryl [beta]-hexosidase was purified 800-fold from bovine liver. The purified enzyme hydrolyzed p-nitrophenyl glycosylpyranoside derivatives of [beta]--galactose, [beta]--glucose, [beta]--xylose, [beta]--mannose, and [alpha]--arabinose, but did not hydrolyze several other p-nitrophenyl glycosides. The enzyme also catalyzed hydrolysis of a variety of plant arylglucosides. Disaccharides, polysaccharides, glycolipids, glycoproteins, and glycosaminoglycans containing terminal nonreducing [beta]--galactopyranosyl or [beta]--glucopyranosyl residues were not hydrolyzed. The pH optima for the several substrates tested ranged from 7.0 to 9.5. The purified enzyme was homogeneous by disc gel electrophoresis and had a molecular weight of 41,000 by Sephadex gel filtration and 46,000 by disc gel electrophoresis performed in the presence of sodium dodecyl sulfate. The enzyme readily transferred glycosyl residues from susceptible [beta]-galactosides or [beta]-glucosides to other sugars; the resulting products were not hydrolyzed by the enzyme. Methyl [alpha]--glucopyranoside was the most efficient carbohydrate acceptor compound tested. The enzyme exhibited a Km for p-nitrophenyl [beta]--galactopyranoside of 1.78 x 10-3 and for p-nitrophenyl [beta]--glucopyranoside, 2.50 x 10-3 when incubations were conducted in the presence of 0.15 methyl [alpha]--glucopyranoside. Aryl [beta]-hexosidase was found in the cytosol of all mammalian livers tested, but could not be detected in liver of birds, reptiles, or fish; low levels were detected in frog liver. Analysis of bovine extracts indicated that the enzyme occurred in liver, kidney, and intestinal mucosa; it was not detected in testis, spleen, serum, or muscle. | en_US |
dc.format.extent | 1484043 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | The purification and properties of an aryl [beta]-hexosidase from bovine liver | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Rackham Arthritis Research Unit and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Rackham Arthritis Research Unit and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.identifier.pmid | 13736 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22995/1/0000563.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(77)90235-1 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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