Reconstitution of apoglucose oxidase with FAD conjugates for biosensoring of progesterone

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 7, 2007, Pages 803-812

  Posthuma Trumpie, Geertruida A ^a,b   van den Berg, Willy A M ^b   van de Wiel, Dirk F M ^b   Schaaper, Wim M M ^c   Korf, Jakob ^a   van Berkel, Willem J H ^b  

^a UNIVERSITY MEDICAL CENTER GRONINGEN   (Netherlands)

^b WAGENINGEN UNIVERSITY   (Netherlands)

^c Pepscan Systems   (Netherlands)

Author keywords

Apoprotein; Biosensor; FAD; Glucose oxidase; Immunoassay; Progesterone

Indexed keywords

6 N (6 AMINOHEXYL)FLAVIN ADENINE NUCLEOTIDE; APOGLUCOSE OXIDASE; APOPROTEIN; DIMER; FLAVINE ADENINE NUCLEOTIDE; GLUCOSE OXIDASE; OLIGOMER; OXIDOREDUCTASE; PROGESTERONE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; ASPERGILLUS NIGER; BIOSENSOR; CONJUGATE; CONJUGATION; DIMERIZATION; ENZYME ACTIVITY; ENZYME RECONSTITUTION; GENETIC RECOMBINATION; HORMONE BINDING; IMMUNOASSAY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STOICHIOMETRY;

APOPROTEINS; ASPERGILLUS NIGER; BIOLOGICAL ASSAY; BIOSENSING TECHNIQUES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, THIN LAYER; DIMERIZATION; FLAVIN-ADENINE DINUCLEOTIDE; FLAVODOXIN; GLUCOSE OXIDASE; IMMUNOASSAY; KINETICS; MODELS, CHEMICAL; OXIDATION-REDUCTION; PROGESTERONE;

ASPERGILLUS NIGER;

EID: 34250885697     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.04.009     Document Type: Article

References (49)

1. Cass A.E.G., Davis G., Francis G.D., Hill H.A., Aston W.J., Higgins I.J., Plotkin E.V., Scott L.D.L., and Turner A.P.F. Ferrocene-mediated enzyme electrode for amperometric determination of glucose. Anal. Chem. 56 (1984) 667-671
2. Bohm S., Pijanowska D., Olthuis W., and Bergveld P. A flow-through amperometric sensor based on dialysis tubing and free enzyme reactors. Biosens. Bioelectron. 16 (2001) 391-397
3. Katz E., Riklin A., Heleg-Shabtai V., Willner I., and Buckmann A.F. Glucose oxidase electrodes via reconstitution of the apo-enzyme: tailoring of novel glucose biosensors. Anal. Chim. Acta 385 (1999) 45-58
4. Rhemrev-Boom R.M., Tiessen R.G., Jonker A.A., Venema K., Vadgama P., and Korf J. A lightweight measuring device for the continuous in vivo monitoring of glucose by means of ultraslow microdialysis in combination with a miniaturised flow-through biosensor. Clin. Chim. Acta 316 (2002) 1-10
5. Urban G., Jobst G., Kohl F., Jachimowicz A., Olcaytug F., Tilado O., Goiser P., Nauer G., Pittner F., Schalkhammer T., and Mann-Buxbaum E. Miniaturized thin-film biosensors using covalently immobilized glucose oxidase. Biosens. Bioelectron. 6 (1991) 555-562
6. Leegsma-Vogt G., Venema K., Brouwer N., Gramsbergen J.B., Copray S., and Korf J. Quantitative on-line monitoring of cellular glucose and lactate metabolism in vitro with slow perfusion. Anal. Chem. 76 (2004) 5431-5435
7. Moser I., Jobst G., Aschauer E., Svasek P., Varahram M., Urban G., Zanin V.A., Tjoutrina G.Y., Zharikova A.V., and Berezov T.T. Miniaturized thin film glutamate and glutamine biosensors. Biosens. Bioelectron. 10 (1995) 527-532
8. Wilson G.S., and Gifford R. Biosensors for real-time in vivo measurements. Biosens. Bioelectron. 20 (2005) 2388-2403
9. Homola J. Present and future of surface plasmon resonance biosensors. Anal. Bioanal. Chem. 377 (2003) 528-539
10. Taitt C.R., Anderson G.P., and Ligler F.S. Evanescent wave fluorescence biosensors. Biosens. Bioelectron. 20 (2005) 2470-2487
11. Morris D.L., Ellis P.B., Carrico R.J., Yeager F.M., Schroeder H.R., Albarella J.P., Boguslaski R.C., Hornby W.E., and Rawson D. Flavin adenine dinucleotide as a label in homogeneous colorimetric immunoassays. Anal. Chem. 53 (1981) 658-665
12. Swoboda B.E.P. The relationship between molecular conformation and the binding of flavin-adenine dinucleotide in glucose oxidase. BBA 175 (1969) 365-379
13. Hefti M.H., Vervoort J., and van Berkel W.J.H. Deflavination and reconstitution of flavoproteins. Tackling fold and function. Eur. J. Biochem. 270 (2003) 4227-4242
14. Morris D.L., and Buckler R.T. In: Langone J.J., and Van Vunakis H. (Eds). Methods in Enzymology vol. 92 (1983), Academic Press, New York 413-425
15. 2 probed using chemically modified flavins bound to glucose oxidase. J. Am. Chem. Soc. 126 (2004) 15120-15131
16. Tyhach R.J., Rupchock P.A., Pendergrass J.H., Skjold A.C., Smith P.J., Johnson R.D., Albarella J.P., and Profitt J.A. Adaptation of prostatic-group-label homogeneous immunoassay to reagent-strip format. Clin. Chem. 27 (1981) 1499-1504
17. Schroeder H.R., Johnson P.K., Dean C.L., Morris D.L., Smith D., and Refetoff S. Homogeneous apoenzyme reactivation immunoassay for thyroxin-binding globulin in serum. Clin. Chem. 32 (1986) 826-830
18. Miles M.V., Tennison M.B., Greenwood R.S., Benoit S.E., Thorn M.D., Messenheimer J.A., and Ehle A.L. Evaluation of the Ames Seralyzer for the determination of carbamazepine, phenobarbital, and phenytoin concentrations in saliva. Ther. Drug Monit. 12 (1990) 501-510
19. Heiss C., Weller M.G., and Niessner R. Dip-and-read test strips for the determination of trinitrotoluene (TNT) in drinking water. Anal. Chim. Acta 396 (1999) 309-316
20. van der Lende T., Schasfoort R.B.M., and van der Meer R.F. Monitoring reproduction using immunological techniques. Anim. Reprod. Sci. 28 (1992) 179-185
21. Claycomb R.W., and Delwiche M.J. Biosensor for on-line measurement of bovine progesterone during milking. Biosens. Bioelectron. 13 (1998) 1173-1180
22. Gillis E.H., Gosling J.P., Sreenan J.M., and Kane M. Development and validation of a biosensor-based immunoassay for progesterone in bovine milk. J. Immunol. Methods 267 (2002) 131-138
23. Kreuzer M., McCarthy R., Pravda M., and Guilbault G. Development of electrochemical immunosensor for progesterone analysis in milk. Anal. Lett. 37 (2004) 943-956
24. Tschmelak J., Kaeppel N., and Gauglitz G. TIRF-based biosensor for sensitive detection of progesterone in milk based on ultra-sensitive progesterone detection in water. Anal. Bioanal. Chem. 382 (2005) 1895-1903
25. Velasco-Garcia M.N., and Mottram T. Biosensors in the livestock industry: an automated ovulation prediction system for dairy cows. Trends Biotechnol. 19 (2001) 433-434
26. Wu Y., Mitchell J., Cook C., and Main L. Evaluation of progesterone-ovalbumin conjugates with different length linkers in enzyme-linked immunosorbant assay and surface plasmon resonance-based immunoassay. Steroids 67 (2002) 565-572
27. Kruip T.A.M., and Spaan W.J.M. In: McFarlaine N.A.A. (Ed). Biotechnological innovations in animal productivity vol. 29 (1992), Butterworth-Heinemann Ltd, Oxford 12-35
28. van Eerdenburg F.J.C.M., Loeffler H.S.H., and van Vliet J.H. Detection of oestrus in dairy cows: a new approach to an old problem. Vet. Q. 18 (1996) 52-54
29. Posthuma-Trumpie G.A., Van den Berg W.A.M., Korf J., and Van Berkel W.J.H. The ninth world congress on biosensors. In: Turner A.P.F. (Ed) (2006), Elsevier, Toronto, CA 275
30. Bückmann A.F., Wray V., and Stocker A. In: McCormick D.B., Suttie J.W., and Wagner C. (Eds). Methods in Enzymology vol. 280 (1997), Academic Press, New York 360-374
31. Beyerman H.C., Hirt J., Kranenburg P., Syrier J.L.M., and Zon A.v. Excess mixed anhydride peptide synthesis with histidine derivatives. Recl. Trav. Chim. Pays-Bas 93 (1974) 256-257
32. van Mierlo C.P.M., van Dongen W.M.A.M., Vergeldt F., van Berkel W.J.H., and Steensma E. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate. Protein Sci. 7 (1998) 2331-2344
33. McIlvaine T.C. A buffer solution for colorimetric comparison. J. Biol. Chem. 49 (1921) 183-186
34. Morris D.L. Effect of antibodies to glucose oxidase in the apoenzyme reactivation immunoassay system. Anal. Biochem. 151 (1985) 235-241
35. Kirchner U., Westphal A.H., Muller R., and van Berkel W.J.H. Phenol Hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD. J. Biol. Chem. 278 (2003) 47545-47553
36. van Berkel W.J.H., Westphal A., Eschrich K., Eppink M., and Kok A. Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Eur. J. Biochem. 210 (1992) 411-419
37. 13C NMR spectra of pregnenolone and progesterone haptens using 2D NMR spectroscopy. Magn. Reson. Chem. 37 (1999) 594-597
38. 13C NMR investigations of glucose oxidase from Aspergillus niger. Eur. J. Biochem. 196 (1991) 663-672
39. Tsuge H., and Mitsuda H. Reconstitution of flavin-adenine dinucleotide in the apoenzyme of glucose oxidase. J. Vitaminol. 17 (1971) 24-31
40. Swoboda B.E.P., and Massey V. Purification and properties of the glucose oxidase from Aspergillus niger. J. Biol. Chem. 240 (1965) 2209-2215
41. Haq S.K., Ahmad M.F., and Khan R.H. The acid-induced state of glucose oxidase exists as a compact folded intermediate. BBRC 303 (2003) 685-692
42. Riklin A., Katz E., Willner I., Stocker A., and Bückmann A.F. Improving enzyme-electrode contacts by redox modification of cofactors. Nature 376 (2002) 672-675
43. Tsuge H., Natsuaki O., and Ohashi K. Purification, properties, and molecular features of glucose oxidase from Aspergillus niger. J. Biochem. (Tokyo) 78 (1975) 835-843
44. Willner I., Heleg-Shabtai V., Blonder R., Katz E., Tao G., Buckmann A.F., and Heller A. Electrical wiring of glucose oxidase by reconstitution of FAD-modified monolayers assembled onto Au-electrodes. J. Am. Chem. Soc. 118 (1996) 10321-10322
45. Zayats M., Katz E., and Willner I. Electrical contacting of glucose oxidase by surface-reconstitution of the apo-protein on a relay-boronic acid-FAD cofactor monolayer. J. Am. Chem. Soc. 124 (2002) 2120-2121
46. Willner I., Blonder R., Katz E., Stocker A., and Buckmann A.F. Reconstitution of apoglucose oxidase with a nitrospiropyran-modified FAD cofactor yields a photoswitchable biocatalyst for amperometric transduction of recorded optical signals. J. Am. Chem. Soc. 118 (1996) 5310-5311
47. Xiao Y., Patolsky F., Katz E., Hainfeld J.F., and Willner I. Plugging into enzymes: nanowiring of redox enzymes by a gold nanoparticle. Science 299 (2003) 1877-1881
48. Hecht H.J., Kalisz H.M., Hendle J., Schmid R.D., and Schomburg D. Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution. J. Mol. Biol. 229 (1993) 153-172
49. Zhu Z., Momeu C., Zakhartsev M., and Schwaneberg U. Making glucose oxidase fit for biofuel cell applications by directed protein evolution. Biosens. Bioelectron. 21 (2006) 2046-2051