Preparing a highly specific inert immunomolecular-magnetic beads for rapid detection and separation of S. aureus and group G Streptococcus

Applied Microbiology and Biotechnology

Volumn 75, Issue 5, 2007, Pages 1209-1216

  Xiao, Xiao ^a   Yang, Xu ^a   Liu, Ting ^a   Chen, Zhang ^a   Chen, Lingli ^a   Li, Huidong ^a   Deng, Le ^a  

^a HUNAN NORMAL UNIVERSITY   (China)

Author keywords

Affinity chromatography interactions; Aldehyde dextran; Detection and separation; Immunomolecular magnetic beads (IMB)

Indexed keywords

AFFINITY CHROMATOGRAPHY; ALDEHYDES; ANTIBODIES; BACTERIA; CELLS; DEXTRAN; IMMUNOSENSORS;

AFFINITY CHROMATOGRAPHY INTERACTIONS; DETECTION AND SEPARATION; IMMUNOMOLECULAR-MAGNETIC BEADS (IMB);

BIOTECHNOLOGY;

ALDEHYDE; DEXTRAN; IMMOBILIZED ANTIBODY;

ADSORPTION; ANTIBODY; BACTERIUM; CHROMATOGRAPHY; DETECTION METHOD; IMMOBILIZATION;

AFFINITY CHROMATOGRAPHY; ANTIGEN ANTIBODY COMPLEX; ARTICLE; BACTERIUM DETECTION; IMMUNOSENSOR; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; REPRODUCIBILITY; SEPARATION TECHNIQUE; STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS GROUP G;

ESCHERICHIA COLI; IMMUNOMAGNETIC SEPARATION; MICROSPHERES; STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS;

STAPHYLOCOCCUS AUREUS; STREPTOCOCCUS SP. 'GROUP G';

EID: 34250687970     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-0921-0     Document Type: Article

References (28)

1. Amit AG, Mariuzza RA, Phillips SEV (1986) Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233:747-753
2. Akerstrom B, Bjorck L (1986) A physicochemical study of protein G. a molecule with unique immunoglobulin G-binding properties. J Biol Chem 261(22):10240-10247
3. Babacam S, Pivarnik P et al (2000) Evaluation of antibody immobilization methods for piezoelectric biosensor application. Biosens Bioelectron. 15:615-621
4. Bjorck L, Kronvall G (1984) Purification and some properties of streptococcal protein G, a novel IgG-binding reagent. J Immunol 133:969-974
5. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
6. Chen LL, Deng L et al (2007) Immunomagnetic separation and MS/SPR end-detection combined procedure for rapid detection of Staphylococcus aureus and protein A. Biosens Bioelectron 22:1487-1492
7. 2 particles containing amine groups. Chin J Biotechnol 20:287-290
8. Cohen-Poradosu R, Jaffe J et al (2004) Group G streptococcal bacteremia in Jerusalem. Emerg Infect Dis 10:1455-1460
9. Danczyk R, Krieder B et al (2003) Comparison of antibody functionality using different immobilization methods. Biotechnol Bioeng 84:215-223
10. Diekema DJ, Pfaller MA et al (2001) Survey of infections due to Staphylococcus species: frequency of occurrence and antimicrobial susceptibility of isolates collected in the United States, Canada, Latin America, Europe, and the Western Pacific region for the SENTRY Antimicrobial Surveillance Program, 1997-1999. Clin Infect Dis 32:114-132
11. Fernandez-Lafuente R, Fuentes M et al (2004) Use of dextrans as spacer arms for oriented covalent immobilization of DNA probes and other ligands at surface of interest in diagnostics. Patent WO 02/072887
12. Fuentes M, Maquiese JV et al (2004) Design of a new cationic exchanger support for reversible immobilization of proteins. Biotechnol Prog 20:284-288
13. Fuentes M, Mateo C et al (2005) Preparation of inert magnetic nano-particles for the directed immobilization of antibodies. Biosens Bioelectron 20:1380-1387
14. Furukawa H, Shimojyo R et al (2003) Affinity selection of target cells from cell surface displayed libraries: a novel procedure using thermo-responsive magnetic nanoparticles. Appl Microbiol Biotechnol 62:478-483
15. Gaber-Porekar V, Menart V (2001) Perspectives of immobilized-metal affinity chromatography. J Biochem Biophys Methods 49:335-360
16. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277:680-685
17. Langone JJ (1982) Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumococci. Adv Immunol 32:157-252
18. Lei H, Deng L et al (2004) The preparation and catalytically active characterization of papain immobilized on magnetic composite microsperes. Enzyme Microb Technol 35:15-21
19. Mansfield LP, Forsythe SJ (2000) The detection of Salmonella using a combined immunomagnetic separation and ELISA end-detection procedure. Lett Microbiol 31:279-283
20. Mateo C, Fernández-Lorente G et al (2000) A new tool to improve the covalent immobilization of proteins: the promotion of physical adsorption of proteins: the promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules 1:739-745
21. Mateo C, Fernández-Lorente G et al (2001a) One step purification, covalent immobilization of poly-his-tagged proteins using novel heterofunctional chelate-epoxy-supports. Biotechnol Bioeng 76:269-277
22. Mateo C, Fernández-Lorente G et al (2001b) Affinity chromatography of poly-His tagged enzymes: a new dextran-coated IMAC matrices for prevention of undesired multipoint adsorptions. J Chromatogr 915:97-106
23. Nice E, Catimel B (1999) Instrumental biosensors: new perspectives for the analysis of biomolecular interactions. BioEssays 12:339-352
24. Pancrazio JJ, Whelan JP et al (1999) Development and application of cell-based biosensors. Ann Biomed Eng 27:697-711
25. Partington KM, Jenkinson EJ, Anderson G (1999) A novel method of cell separation based on dual parameter immunomagnetic cell selection. J Immunol Methods 223:195-205
26. Pessela BCC, Mateo C et al (2003) One-step purification, covalent immobilization, and additional stabilization of a thermophilic poly-His-tagged-galactosidase from Thermus sp. Strain T2 by using novel heterofunctional chelate-epoxy sepabeads. Biomacromolecules 4:107-113
27. Shinkai M et al (2002) Functional magnetic particles for medical application. J Biosci Bioeng 94:606-613
28. Turkova J (1999) Oriented immobilization of biologically active proteins as a tool for revealing protein interactions and function. J Chromatogr B 722:11-31