Linked Life Data

9460552

Source:http://linkedlifedata.com/resource/pubmed/id/9460552

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-3-23
pubmed:abstractText
In this investigation, a comparison of wild type recombinant streptavidin (r-SAv) with two genetically engineered mutant r-SAv proteins was undertaken. The investigation also included a comparison of the r-SAv with two streptavidin (SAv) proteins from commercial sources. In vitro characterization of the SAv proteins was conducted by HPLC, SDS-PAGE, IEF, and electrospray mass spectral analyses. All SAv proteins studied appeared to be a single species by size exclusion chromatography (HPLC) and SDS-PAGE analyses, but multiple species were noted in the IEF and MS analyses. In vivo comparisons of the SAv proteins were accomplished with dual isotope-labeled SAv in athymic mice. In an initial experiment, tissue localization of r-[131I]SAv directly radiolabeled using chloramine-T was compared with r-SAv radiolabeled with the N-hydroxysuccinimidyl p-iodobenzoate conjugate ([125I]-PIB), a radioiodination reagent that has been shown to result in iodine-labeled proteins which are stable to in vivo deiodination. The data obtained indicated that there is little difference in the distribution (except kidney localization) when r-SAv labeled by the two methods. Data obtained from comparison of r-[131I]SAv with a disulfide-stabilized r-SAv mutant (r-SAv-H127C), a C-terminal cysteine-containing r-SAv mutant (r-[125I]SAv-S139C), and two 125I-labeled SAv proteins obtained from commercial sources indicated that their distributions were quite similar, except the kidney concentrations were generally lower than that of r-[131I]SAv. On the basis of the similar distributions of the SAv proteins studied, it appears that the r-SAv mutants may be interchanged for the (wild type) r-SAv in pretargeting studies. Further, the similarity of distributions with two commercially available SAv proteins suggests that the results obtained in our studies and those of other groups may be directly compared (with consideration of animal model, sacrifice time, etc.).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1043-1802
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
100-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9460552-Animals, pubmed-meshheading:9460552-Chloramines, pubmed-meshheading:9460552-Chromatography, High Pressure Liquid, pubmed-meshheading:9460552-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:9460552-Immunotoxins, pubmed-meshheading:9460552-Indicators and Reagents, pubmed-meshheading:9460552-Iodine Radioisotopes, pubmed-meshheading:9460552-Isoelectric Focusing, pubmed-meshheading:9460552-Isotope Labeling, pubmed-meshheading:9460552-Kidney, pubmed-meshheading:9460552-Male, pubmed-meshheading:9460552-Mass Spectrometry, pubmed-meshheading:9460552-Mice, pubmed-meshheading:9460552-Mice, Nude, pubmed-meshheading:9460552-Mutagenesis, pubmed-meshheading:9460552-Protein Engineering, pubmed-meshheading:9460552-Recombinant Proteins, pubmed-meshheading:9460552-Streptavidin, pubmed-meshheading:9460552-Tosyl Compounds
pubmed:articleTitle
Streptavidin in antibody pretargeting. Comparison of a recombinant streptavidin with two streptavidin mutant proteins and two commercially available streptavidin proteins.
pubmed:affiliation
Department of Radiation Oncology, University of Washington, Seattle 98195, USA. dswilbur@u.washington.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't