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Bovine testicular [beta]-galactosidase: Purification of enzyme fractions that exhibit high affinity for phosphomannosyl receptors

dc.contributor.authorDistler, Jack J.en_US
dc.contributor.authorGuo, Jinfengen_US
dc.contributor.authorSahagian, G. Garyen_US
dc.contributor.authorJourdian, George W.en_US
dc.date.accessioned2006-04-07T20:39:52Z
dc.date.available2006-04-07T20:39:52Z
dc.date.issued1989-11-01en_US
dc.identifier.citationDistler, Jack J., Guo, Jinfeng, Sahagian, G. Gary, Jourdian, George W. (1989/11/01)."Bovine testicular [beta]-galactosidase: Purification of enzyme fractions that exhibit high affinity for phosphomannosyl receptors." Analytical Biochemistry 182(2): 432-437. <http://hdl.handle.net/2027.42/27707>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6W9V-4DX4FTM-1XS/2/85a0f6a760d3fcc9a43d85b3cc38e2a3en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/27707
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2558593&dopt=citationen_US
dc.description.abstractAn improved method is described for the preparation of bovine testicular [beta]-galactosidase that allows the isolation of enzyme fractions that bind avidly to phosphomannosyl receptors. The procedure permits removal of a contaminating [beta]-hexosaminidase and yields nearly homogeneous [beta]-galactosidase. Enzyme eluted from DEAE-Sephacel was arbitrarily divided into pools that exhibited differing ability to bind phosphomannosyl receptors. A high binding fraction was rapidly assimilated by cultured cells and bound to both low and high molecular weight phosphomannosyl receptors. Carbohydrate analysis of the high binding fraction indicates an average content of one complex and one high mannose oligosaccharide chain per molecule and an average mannose 6-phosphate content of two residues per molecule. However, electrofocusing studies indicated that all the fractions were heterogeneous with respect to sialic acid and phosphate content. The purification procedure also provides highly purified [beta]-galactosidase suitable for removing [beta]-galactosidase residues from a variety of complex carbohydrates.en_US
dc.format.extent715993 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleBovine testicular [beta]-galactosidase: Purification of enzyme fractions that exhibit high affinity for phosphomannosyl receptorsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Rackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Rackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Rackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.en_US
dc.contributor.affiliationumRackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA; Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.en_US
dc.identifier.pmid2558593en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/27707/1/0000093.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-2697(89)90619-2en_US
dc.identifier.sourceAnalytical Biochemistryen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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