Bovine testicular [beta]-galactosidase: Purification of enzyme fractions that exhibit high affinity for phosphomannosyl receptors
dc.contributor.author | Distler, Jack J. | en_US |
dc.contributor.author | Guo, Jinfeng | en_US |
dc.contributor.author | Sahagian, G. Gary | en_US |
dc.contributor.author | Jourdian, George W. | en_US |
dc.date.accessioned | 2006-04-07T20:39:52Z | |
dc.date.available | 2006-04-07T20:39:52Z | |
dc.date.issued | 1989-11-01 | en_US |
dc.identifier.citation | Distler, 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.uri | http://www.sciencedirect.com/science/article/B6W9V-4DX4FTM-1XS/2/85a0f6a760d3fcc9a43d85b3cc38e2a3 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/27707 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2558593&dopt=citation | en_US |
dc.description.abstract | An 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.extent | 715993 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 | Bovine testicular [beta]-galactosidase: Purification of enzyme fractions that exhibit high affinity for phosphomannosyl receptors | 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 | 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; Rackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. | en_US |
dc.contributor.affiliationum | 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; Rackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. | en_US |
dc.contributor.affiliationum | 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; Rackham Arthritis Research Unit, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. | en_US |
dc.contributor.affiliationum | Rackham 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.pmid | 2558593 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/27707/1/0000093.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-2697(89)90619-2 | en_US |
dc.identifier.source | Analytical Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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