The aggregation and dissociation properties of a low molecular weight mannose 6-phosphate receptor from bovine testis
dc.contributor.author | Li, Maomi | en_US |
dc.contributor.author | Distler, Jack J. | en_US |
dc.contributor.author | Jourdian, George W. | en_US |
dc.date.accessioned | 2006-04-10T13:33:37Z | |
dc.date.available | 2006-04-10T13:33:37Z | |
dc.date.issued | 1990-11-15 | en_US |
dc.identifier.citation | Li, Maomi, Distler, Jack J., Jourdian, George W. (1990/11/15)."The aggregation and dissociation properties of a low molecular weight mannose 6-phosphate receptor from bovine testis." Archives of Biochemistry and Biophysics 283(1): 150-157. <http://hdl.handle.net/2027.42/28309> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DPC28S-16H/2/a2be1ec8ce523076e10e4f985821b9c5 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28309 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2173489&dopt=citation | en_US |
dc.description.abstract | The aggregation state of low molecular weight mannose 6-phosphate receptor from bovine testis was determined in membrane preparations and in purified soluble preparations. The effect of aggregation on binding of the receptor to immobilized pentamannose 6-phosphate was also examined. Nonreducing SDS--PAGE followed by immunoblotting revealed that interchain disulfide bonds exist in detergent-solubilized and purified receptor preparations, but not in membrane-associated receptor. Reduction of the receptor with dithiothreitol abolished its ligand binding activity and drastically altered its ability to bind antibodies. The results of receptor crosslinking and molecular sieving chromatography studies suggest that the receptor exists in membranes as a noncovalently linked dimer and in solution as oligomeric forms, largely as a tetramer. The formation of the tetramer is affected by the concentration of the receptor, but not by its solubilization from membranes with detergent, nor by the presence of mannose 6-phosphate. Mono-, di- and tetramer forms of 125I-labeled receptor were separated by molecular sieving chromatography and examined for their ability to bind to immobilized ligand, agarose-pentamannosephosphate. The order of binding observed was tetramer > dimer > monomer. Binding of the monomer and dimer to immobilized ligand was dependent on the presence of divalent cations while the tetramer had little requirement for divalent cations. | en_US |
dc.format.extent | 1670447 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 aggregation and dissociation properties of a low molecular weight mannose 6-phosphate receptor from bovine testis | 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, and the Rackham Arthritis Research Unit, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, and the Rackham Arthritis Research Unit, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, and the Rackham Arthritis Research Unit, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.identifier.pmid | 2173489 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28309/1/0000063.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(90)90625-9 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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