A new procedure for the synthesis of polyethylene glycol-protein adducts; Effects on function, receptor recognition, and clearance of superoxide dismutase, lactoferrin, and [alpha]2-macroglobulin
dc.contributor.author | Beauchamp, Charles O. | en_US |
dc.contributor.author | Gonias, Steven L. | en_US |
dc.contributor.author | Menapace, David P. | en_US |
dc.contributor.author | Pizzo, Salvatore V. | en_US |
dc.date.accessioned | 2006-04-07T18:42:44Z | |
dc.date.available | 2006-04-07T18:42:44Z | |
dc.date.issued | 1983-05 | en_US |
dc.identifier.citation | Beauchamp, Charles O., Gonias, Steven L., Menapace, David P., Pizzo, Salvatore V. (1983/05)."A new procedure for the synthesis of polyethylene glycol-protein adducts; Effects on function, receptor recognition, and clearance of superoxide dismutase, lactoferrin, and [alpha]2-macroglobulin." Analytical Biochemistry 131(1): 25-33. <http://hdl.handle.net/2027.42/25222> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6W9V-4DV0B9X-44/2/11547a6d4d21622d93be4b995ecdfb48 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/25222 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6193731&dopt=citation | en_US |
dc.description.abstract | A new, simplified technique for the synthesis of polyethylene glycol (PEG) derivatives of proteins utilizing 1,1'-carbonyldiimidazole for PEG activation, is described. PEG derivatives of superoxide dismutase, [alpha]2-macroglobulin, [alpha]2-macroglobulin-trypsin, and lactoferrin were prepared and studied. Superoxide dismutase coupled to PEG preserved 95% of its original activity while its plasma half-life increased from 3.5 min to 9 or more hours depending on the PEG derivative studied. PEG-derivatized [alpha]2-macroglobulin showed decreased protease binding activity but PEG derivatives of preformed [alpha]2-macroglobulin-trypsin demonstrated no loss of activity. The plasma clearance of PEG-[alpha]2-macroglobulin-trypsin was prolonged significantly compared to native [alpha]2-macroglobulin-trypsin, particularly when a high-molecular-weight PEG was coupled to the protease inhibitor complex. The plasma clearance half-life of lactoferrin was increased 5-to 20-fold by this modification. Trinitrobenzenesulfonic acid titration studies demonstrated that [epsilon]-amino groups of lysine residues are modified by the coupling of carbonyldiimidazole-activated PEG to proteins. | en_US |
dc.format.extent | 1236373 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 | A new procedure for the synthesis of polyethylene glycol-protein adducts; Effects on function, receptor recognition, and clearance of superoxide dismutase, lactoferrin, and [alpha]2-macroglobulin | 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 | The Ann Arbor Veterans Administration Hospital, Ann Arbor, Michigan 48105, USA; The Department of Medicine, University of Michigan, Ann Arbor, Michigan 48105, USA | en_US |
dc.contributor.affiliationum | The Ann Arbor Veterans Administration Hospital, Ann Arbor, Michigan 48105, USA; The Department of Medicine, University of Michigan, Ann Arbor, Michigan 48105, USA | en_US |
dc.contributor.affiliationother | The Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA; Department of Pathology, Duke University Medical Center, Durham, North Carolina 27710, USA | en_US |
dc.contributor.affiliationother | The Department of Pathology, Duke University Medical Center, Durham, North Carolina 27710, USA; The Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA | en_US |
dc.identifier.pmid | 6193731 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/25222/1/0000663.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-2697(83)90131-8 | en_US |
dc.identifier.source | Analytical Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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