Streptavidin-biotinylated IgG conjugates: a simple procedure for reducing polymer formation
dc.contributor.author | Del Rosario, Renato B. | en_US |
dc.contributor.author | Baron, Lee Ann | en_US |
dc.contributor.author | Lawton, Richard G. | en_US |
dc.contributor.author | Wahl, Richard L. | en_US |
dc.date.accessioned | 2006-04-10T15:17:00Z | |
dc.date.available | 2006-04-10T15:17:00Z | |
dc.date.issued | 1992-04 | en_US |
dc.identifier.citation | Del Rosario, Renato B., Baron, Lee Ann, Lawton, Richard G., Wahl, Richard L. (1992/04)."Streptavidin-biotinylated IgG conjugates: a simple procedure for reducing polymer formation." International Journal of Radiation Applications and Instrumentation. Part B. Nuclear Medicine and Biology 19(3): 417-421. <http://hdl.handle.net/2027.42/30136> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B7GH9-4C00NKP-7J/2/3ad1f8076fe5ab73e620d436cff678c5 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/30136 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1629031&dopt=citation | en_US |
dc.description.abstract | Disulfide links of the IgG2ak anti-ovarian carcinoma antibody, 5G6.4, were site-specifically biotinylated [[approximate]2 biotins/ IgG2a] using a novel crosslinking procedure using the biotin derivatized ETAC (equilibrium transfer alkylation crosslink reagent) 1a. Complexation of ETAC 1a biotinylated 5G6.4 on a column of immobilized protein A at high dilution, followed by passage of [125I]streptavidin, washing and pH change leads to elution of a streptavidin-free product with a molecular mass in the 200-300 kDa range. By contrast, direct mixing with [125I]streptavidin rapidly gave larger oligomers of >>669 and [approximate]440-669 kDa molecular mass, respectively. The biodistribution of the 200-300 kDa complex showed significantly diminished liver, kidney and spleen uptake as well as higher blood activity than the 440-669 kDa complex. The methodology represent the first application of ETAC chemistry to disulfide-bond directed biotinylation of antibodies and the synthesis of streptavidin antibody conjugates which minimizes their polymerization. | en_US |
dc.format.extent | 441030 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 | Streptavidin-biotinylated IgG conjugates: a simple procedure for reducing polymer formation | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Physics | en_US |
dc.subject.hlbsecondlevel | Nuclear Engineering and Radiological Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Division of Nuclear Medicine-Internal Medicine, University of Michigan Medical Center, Ann Arbor, MI 48109-0028, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan Medical Center, Ann Arbor, MI 48109-0028, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan Medical Center, Ann Arbor, MI 48109-0028, U.S.A. | en_US |
dc.contributor.affiliationum | Division of Nuclear Medicine-Internal Medicine, University of Michigan Medical Center, Ann Arbor, MI 48109-0028, U.S.A. | en_US |
dc.identifier.pmid | 1629031 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/30136/1/0000513.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0883-2897(92)90128-L | en_US |
dc.identifier.source | International Journal of Radiation Applications and Instrumentation. Part B. Nuclear Medicine and Biology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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