Aldehyde–dextran–protein conjugates to immobilize amino-haptens: avoiding cross-reactions in the immunodetection
Explore this paper's citation graph
Summary
It has been found that the use of dextran–protein carriers conjugates avoid the high cross-reaction found using the carbodiimide routes.
- Type
- article
- Published
- 2005-03-02
- Cited by
- 10
- References
- 28
- OpenAlex
- https://openalex.org/W1964352874
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:84010802
Keywords
Hapten, Carbodiimide, Conjugate, Dextran, Chemistry
References
- Antisera specificities to 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide adducts of proteins.
- Practice and theory of enzyme immunoassays
- The use of carbodiimides in the preparation of immunizing conjugates.
- Laboratory techniques in biochemistry and molecular biology
- New Cationic Exchanger Support for Reversible Immobilization of Proteins
- Autoantibodies directed against ribosomal P proteins: use of a multiple antigen peptide as the coating agent in ELISA.
- Determination of protein‐protein interactions through aldehyde‐dextran intermolecular cross‐linking
- Synthesis and characterization of some modified polysaccharides containing drug moieties
- Grafting peptides onto polystyrene microplates for ELISA.
- Hydrocoating: a new method for coupling biomolecules to solid phases.
- Targeted drug conjugates: principles and progress.
- Covalent linking of haptens, proteins and nucleic acids to a modified polystyrene support.
- Aldo-enol transition in periodate-oxidized dextrans
- Uncertainties in the use of periodate oxidation for determination of dextran structure.
- Directed covalent immobilization of aminated DNA probes on aminated plates.
- Multi-well ELISA based on independent peptide antigens for antibody capture. Application to Lyme disease serodiagnosis.
- Effective method for synthetic peptide immobilization that increases the sensitivity and specificity of ELISA procedures.
- An improved 2,4,6-trinitrobenzenesulfonic acid method for the determination of amines.
- An investigation of the structure of periodate-oxidised dextran
- Dextran, a hapten carrier in immunoassays for s-triazines. A comparison with ELISAs based on hapten-protein conjugates.
Cited by
- Detection of polyclonal antibody against any area of the protein-antigen using immobilized protein-antigens: the critical role of the immobilization protocol.
- The use of glycidol to introduce aldehyde functions into proteins - Application to the fluorescent labelling of bovine serum albumin and avidin
- Optimization of the modification of carrier proteins with aminated haptens.
- Preparation of Dextran Modified Superparamagnetic Iron Oxide Nanoparticles Based Immunoprobes
- A ROLE FOR INTERLEUKIN-17A AS A MEDIATOR OF SYMPATHETIC NEUROANATOMICAL REMODELLING DURING EXPERIMENTAL COLITIS
- Polysaccharide-based materials in macromolecular prodrug design and development
- Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System
- Recent advances in dextran-based drug delivery systems: From fabrication strategies to applications.
- Native/modified dextran-based nanogel in delivering drug and management of ocular complications: a review
- Functional Polymers Based on Dextran
Related papers
- Structural and functional properties of sodium caseinate glycosylated by dextran aldehyde.
- Macromolecular contrast agents for magnetic resonance imaging. Influence of polymer content in ligand on the paramagnetic properties.
- Chemical modification of Aspergillus 1,2-α-d-mannosidase by water-soluble carbodiimide
- New antibody purification procedure using a thermally responsive poly(N-isopropylacrylamide)-dextran derivative conjugate.
- Effect of chemical modification with carboxymethyl dextran on kinetic and structural properties of L-asparaginase.
- Glycosidation of cu,zn-superoxide dismutase with end-group aminated dextran: pharmacological and pharmacokinetics properties.
- Irreversible thermoinactivation of glucoamylase from Aspergillus niger and thermostabilization by chemical modification of carboxyl groups.
- Modification of carboxyl groups in the active site of trypsin.