دورية أكاديمية
Linear gene fusions of antibody fragments with streptavidin can be linked to biotin labelled secondary molecules to form bispecific reagents.
العنوان: | Linear gene fusions of antibody fragments with streptavidin can be linked to biotin labelled secondary molecules to form bispecific reagents. |
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المؤلفون: | Pearce LA; CSIRO, Division of Biomolecular Engineering, Parkville, Australia., Oddie GW, Coia G, Kortt AA, Hudson PJ, Lilley GG |
المصدر: | Biochemistry and molecular biology international [Biochem Mol Biol Int] 1997 Sep; Vol. 42 (6), pp. 1179-88. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Taylor & Francis Country of Publication: England NLM ID: 9306673 Publication Model: Print Cited Medium: Print ISSN: 1039-9712 (Print) Linking ISSN: 10399712 NLM ISO Abbreviation: Biochem Mol Biol Int Subsets: MEDLINE |
أسماء مطبوعة: | Publication: 1999: London ; Philadelphia, PA : Taylor & Francis Original Publication: Sydney ; New York : Academic Press, c1993-c1999. |
مواضيع طبية MeSH: | Biotin/*chemistry , Immunoglobulin Light Chains/*genetics , Immunoglobulin Variable Region/*genetics , Recombinant Fusion Proteins/*genetics , Streptavidin/*genetics, Animals ; Antibodies ; Antibodies, Bispecific/genetics ; Antibodies, Bispecific/metabolism ; Artificial Gene Fusion/methods ; Biosensing Techniques ; Escherichia coli/genetics ; Immunoglobulin Fragments/chemistry ; Immunoglobulin Fragments/genetics ; Immunoglobulin Fragments/metabolism ; Immunoglobulin Light Chains/chemistry ; Immunoglobulin Light Chains/metabolism ; Immunoglobulin Variable Region/chemistry ; Immunoglobulin Variable Region/metabolism ; Influenza A virus/enzymology ; Mice ; Neuraminidase/immunology ; Recombinant Fusion Proteins/immunology ; Recombinant Fusion Proteins/metabolism ; Streptavidin/chemistry ; Streptavidin/metabolism |
مستخلص: | Monomeric single chain antibody (scFv) fragments lack both the avidity of the bivalent IgG, or (Fab')2 fragment, and the effector functions conferred by the Fc domain. For certain diagnostic or therapeutic applications it may be desirable to link these molecules to other proteins, antibodies, enzymes or peptide ligands, and chemical or recombinant methods have been developed to produce many of these crosslinked reagents. One approach has been to link an antibody fragment to streptavidin which can bind a second biotinylated molecule to create a higher affinity, bifunctional or bispecific molecule. To demonstrate the applicability of this technology, an anti-neuraminidase NC10 scFv-streptavidin fusion was expressed in E. coli and the product was refolded and purified to homogeneity from 6 M guanidine hydrochloride. Analysis in a BIAcore biosensor showed that the NC10 scFv moiety reacted with immobilised neuraminidase and that the core streptavidin moiety was able to bind biotinylated anti-ferritin Fab' to produce a new model bispecific reagent which bound ferritin. Conceptually, this design principle can be applied to the creation of useful diagnostic and possibly therapeutic molecules. |
المشرفين على المادة: | 0 (Antibodies) 0 (Antibodies, Bispecific) 0 (Immunoglobulin Fragments) 0 (Immunoglobulin Light Chains) 0 (Immunoglobulin Variable Region) 0 (Recombinant Fusion Proteins) 6SO6U10H04 (Biotin) 9013-20-1 (Streptavidin) EC 3.2.1.18 (Neuraminidase) |
تواريخ الأحداث: | Date Created: 19970926 Date Completed: 19971103 Latest Revision: 20191024 |
رمز التحديث: | 20221213 |
DOI: | 10.1080/15216549700203651 |
PMID: | 9305536 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1039-9712 |
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DOI: | 10.1080/15216549700203651 |