Detergent dissociation of bovine liver phosphomannosyl binding protein
dc.contributor.author | Mitchell, Diane C. | en_US |
dc.contributor.author | Maler, Thomas | en_US |
dc.contributor.author | Jourdian, George W. | en_US |
dc.date.accessioned | 2006-04-28T16:58:29Z | |
dc.date.available | 2006-04-28T16:58:29Z | |
dc.date.issued | 1984 | en_US |
dc.identifier.citation | Mitchell, Diane C.; Maler, Thomas; Jourdian, George W. (1984)."Detergent dissociation of bovine liver phosphomannosyl binding protein." Journal of Cellular Biochemistry 24(4): 319-330. <http://hdl.handle.net/2027.42/38443> | en_US |
dc.identifier.issn | 0730-2312 | en_US |
dc.identifier.issn | 1097-4644 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/38443 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6088561&dopt=citation | en_US |
dc.description.abstract | We have reported previously the isolation and partial characterization of a 215-kilodalton (Kd) phosphomannosyl binding protein from bovine liver membranes [3,9]. In the present studies evidence is presented that the binding protein is an aggregate. Four N-terminal amino acids were detected, and the complex could be dissociated into subunits. Bovine liver membranes were extracted with the detergent, Zwittergent, in the presence of protease inhibitors. The extract was subjected to affinity chromatography on phosphomannan-Sepharose 4B, and proteins with apparent M r values of 215 and 57 Kd were eluted with mannose 6-phosphate. As reported previously, extraction with Triton X-100 yielded only the higher molecular weight material. When the binding protein was incubated at 4°C in the presence of Zwittergent TM 3-14 the 215-Kd form slowly dissociated into smaller subunits; after two months, the major species had an apparent M r of 57 Kd. The subunits derived from the binding protein were recognized by antiserum raised against purified binding protein. Dissociation of the binding protein by Zwittergent was enhanced by incubation at 37°C, the presence of dithiothreitol, and low pH values. The subunit mixture enriched in the 57-Kd subunit had a lowered ability to bind ligands containing the phosphomannosyl recognition marker. Binding was partially restored (>48% of the initial value) when dissociated receptor was back exchanged with Triton X-100. | en_US |
dc.format.extent | 1414516 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.subject.other | Cell & Developmental Biology | en_US |
dc.title | Detergent dissociation of bovine liver phosphomannosyl binding protein | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Rackham Arthritis Research Unit, University of Michigan School of Medicine, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Rackham Arthritis Research Unit, University of Michigan School of Medicine, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry and Internal Medicine, University of Michigan School of Medicine, Ann Arbor, Michigan 48109 ; Department of Rackham Arthritis Research Unit, University of Michigan School of Medicine, Ann Arbor, Michigan 48109 | en_US |
dc.identifier.pmid | 6088561 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/38443/1/240240403_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/jcb.240240403 | en_US |
dc.identifier.source | Journal of Cellular Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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