Identification of bacterial glycosidases in rat cecal contents
dc.contributor.author | Prizont, Roberto | en_US |
dc.contributor.author | Konigsberg, Nancy | en_US |
dc.date.accessioned | 2006-09-11T14:43:57Z | |
dc.date.available | 2006-09-11T14:43:57Z | |
dc.date.issued | 1981-09 | en_US |
dc.identifier.citation | Prizont, Roberto; Konigsberg, Nancy; (1981). "Identification of bacterial glycosidases in rat cecal contents." Digestive Diseases and Sciences 26(9): 773-777. <http://hdl.handle.net/2027.42/44391> | en_US |
dc.identifier.issn | 0163-2116 | en_US |
dc.identifier.issn | 1573-2568 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44391 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6793336&dopt=citation | en_US |
dc.description.abstract | Cecal contents of conventional and germfree rats were examined for glycosidases which may have a role in degrading glycoprotein oligosaccharides. Utilizing p-nitrophenylglycosides as substrates, we identified glycosidases in bacteria-free supernatants from cecal contents which act on β-linkages. These cecal glycosidases appear to be of bacterial origin since: (1) direct comparisons of the enzymes in similar contents from germfree rats showed negligible activities; (2) most of the glycosidase levels in bacterial extracts were at least as high as those of soluble supernatants; and (3) disk gel electrophoresis of contents and bacterial extracts revealed in both preparations a β- N -acetylglucosaminidase band with similar R f s. Also, the blood group B antigenicity of germfree cecal glycoproteins was greatly decreased by conventional cecal contents. These findings indicate that β-galactosidase and β- N -acetylgalactosaminidase in cecal contents are bacterial in origin, and they may have a role in the bacterial catabolism of intestinal glycoproteins. | en_US |
dc.format.extent | 461734 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Digestive Disease Systems, Inc. ; Springer Science+Business Media | en_US |
dc.subject.other | Transplant Surgery | en_US |
dc.subject.other | Medicine & Public Health | en_US |
dc.subject.other | Gastroenterology | en_US |
dc.subject.other | Hepatology | en_US |
dc.subject.other | Oncology | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.title | Identification of bacterial glycosidases in rat cecal contents | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Internal Medicine and Specialties | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, Gastrointestinal Research Division, University of Michigan, 48109, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, Gastrointestinal Research Division, University of Michigan, 48109, Ann Arbor, Michigan; Veterans Administration Medical Center, 87108, Albuquerque, New Mexico | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 6793336 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44391/1/10620_2005_Article_BF01309607.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF01309607 | en_US |
dc.identifier.source | Digestive Diseases and Sciences | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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