Tamavidin, a versatile affinity tag for protein purification and immobilization

Journal of Biotechnology

Volumn 145, Issue 4, 2010, Pages 317-322

  Takakura, Yoshimitsu ^a   Oka, Naomi ^a   Kajiwara, Hitomi ^a   Tsunashima, Masako ^a   Usami, Satoru ^a   Tsukamoto, Hiroshi ^a   Ishida, Yuji ^a   Yamamoto, Takeshi ^a  

^a JAPAN TOBACCO INC   (Japan)

Author keywords

Affinity tag; Avidin; Biotin; Escherichia coli; Immobilization; Purification

Indexed keywords

AFFINITY TAG; AVIDIN; AVIDIN-BIOTIN; BINDING PROTEINS; BY-2 CELL; E. COLI; EFFICIENT SYSTEMS; FUSION PROTEINS; FUSION TECHNOLOGY; HIGH AFFINITY; HIGH LEVEL EXPRESSION; MAGNETIC MICROBEADS; MICROBEADS; ONE-STEP PURIFICATION; PROTEIN PURIFICATION; RECOMBINANT HOSTS; RECOMBINANT PROTEIN; SOYBEAN AGGLUTININS; STREPTAVIDIN; TOBACCO BY-2 CELLS;

BACTERIOLOGY; CELL CULTURE; COENZYMES; ESCHERICHIA COLI; PURIFICATION;

PROTEINS;

AVIDIN; BIOTIN; HYBRID PROTEIN; RECOMBINANT PROTEIN; SIALYLTRANSFERASE; SIALYLTRANSFERASE TAMAVIDIN 2 FUSION PROTEIN; SOYBEAN AGGLUTININ; SOYBEAN AGGLUTININ TAMAVIDIN 2 FUSION PROTEIN; TAMAVIDIN 2; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM CULTURE; BINDING AFFINITY; BIOTECHNOLOGY; CELL CULTURE; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PLANT CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN IMMOBILIZATION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; TOBACCO;

AVIDIN; BIOTECHNOLOGY; BIOTIN; CARRIER PROTEINS; ESCHERICHIA COLI; FUNGAL PROTEINS; IMMOBILIZED PROTEINS; KINETICS; MICROSPHERES; MOLECULAR SEQUENCE DATA; PLANT LECTINS; RECOMBINANT FUSION PROTEINS; SIALYLTRANSFERASES; SOYBEAN PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; GLYCINE MAX; NICOTIANA TABACUM;

EID: 77049127501     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.12.012     Document Type: Article

References (31)

1. Adar R., Sharon N. Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin. Eur. J. Biochem. 1996, 239:668-674.
2. Adar R., Streicher H., Rozenblatt S., Sharon N. Synthesis of soybean agglutinin in bacterial and mammalian cells. Eur. J. Biochem. 1997, 249:684-689.
3. Airenne K.J., Kulomaa M.S. Rapid purification of recombinant proteins fused to chicken avidin. Gene 1995, 167:63-68.
4. Airenne K.J., Laitinen O.H., Alenius H., Mikkola J., Kalkkinen N., Arif S.A., Yeang H.Y., Palosuo T., Kulomaa M.S. Avidin is a promising tag for fusion proteins produced in baculovirus-infected insect cells. Protein Expr. Purif. 1999, 17:139-145.
5. Airenne K.J., Marjomaki V.S., Kulomaa M.S. Recombinant avidin and avidin-fusion proteins. Biomol. Eng. 1999, 16:87-92.
6. Arnau J., Lauritzen C., Petersen G.E., Pedersen J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr. Purif. 2006, 48:1-13.
7. Boado R.J., Zhang Y., Xia C.F., Wang Y., Pardridge W.M. Genetic engineering, expression, and activity of a chimeric monoclonal antibody-avidin fusion protein for receptor-mediated delivery of biotinylated drugs in humans. Bioconjug. Chem. 2008, 19:731-739.
8. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
9. Clare D.A., Valentine V.W., Catignani G.L., Swaisgood H.E. Molecular design, expression, and affinity immobilization of a trypsin-streptavidin fusion protein. Enzyme Microb. Technol. 2001, 28:483-491.
10. Green N.M. Avidin and streptavidin. Methods Enzymol. 1990, 184:51-67.
11. Hiei Y., Ohta S., Komari T., Kumashiro T. Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. Plant J. 1994, 6:271-282.
12. Hood E.E., Kusnadi A., Nikolov Z., Howard J.A. Molecular farming of industrial proteins from transgenic maize. Adv. Exp. Med. Biol. 1999, 464:127-147.
13. Karp M., Lindqvist C., Nissinen R., Wahlbeck S., Akerman K., Oker-Blom C. Identification of biotinylated molecules using a baculovirus-expressed luciferase-streptavidin fusion protein. Biotechniques 1996, 20:452-456.
14. Kipriyanov S.M., Little M., Kropshofer H., Breitling F., Gotter S., Dubel S. Affinity enhancement of a recombinant antibody: formation of complexes with multiple valency by a single-chain Fv fragment-core streptavidin fusion. Protein Eng. 1996, 9:203-211.
15. Komari T., Hiei Y., Saito Y., Murai N., Kumashiro T. Vectors carrying two separate T-DNAs for co-transformation of higher plants mediated by Agrobacterium tumefaciens and segregation of transformants free from selection markers. Plant J. 1996, 10:165-174.
16. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
17. Li J.Y., Sugimura K., Boado R.J., Lee H.J., Zhang C., Duebel S., Pardridge W.M. Genetically engineered brain drug delivery vectors: cloning, expression and in vivo application of an anti-transferrin receptor single chain antibody-streptavidin fusion gene and protein. Protein Eng. 1999, 12:787-796.
18. Murray C., Sutherland P.W., Phung M.M., Lester M.T., Marshall R.K., Christeller J.T. Expression of biotin-binding proteins, avidin and streptavidin, in plant tissues using plant vacuolar targeting sequences. Transgenic Res. 2002, 11:199-214.
19. Ng P.P., Dela Cruz J.S., Sorour D.N., Stinebaugh J.M., Shin S.U., Shin D.S., Morrison S.L., Penichet M.L. An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:10706-10711.
20. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual 1989, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 2nd ed.
21. Sano T., Cantor C.R. A streptavidin-protein A chimera that allows one-step production of a variety of specific antibody conjugates. Biotechnology (NY) 1991, 9:1378-1381.
22. Sano T., Cantor C.R. Streptavidin-containing chimeric proteins: design and production. Methods Enzymol. 2000, 326:305-311.
23. Sano T., Glazer A.N., Cantor C.R. A streptavidin-metallothionein chimera that allows specific labeling of biological materials with many different heavy metal ions. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:1534-1538.
24. Shin S.U., Wu D., Ramanathan R., Pardridge W.M., Morrison S.L. Functional and pharmacokinetic properties of antibody-avidin fusion proteins. J. Immunol. 1997, 158:4797-4804.
25. Smith M.C., Furman T.C., Ingolia T.D., Pidgeon C. Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins. J. Biol. Chem. 1988, 263:7211-7215.
26. Takakura Y., Tsunashima M., Suzuki J., Usami S., Kakuta Y., Okino N., Ito M., Yamamoto T. Tamavidins-novel avidin-like biotin-binding proteins from the Tamogitake mushroom. FEBS J. 2009, 276:1383-1397.
27. Tsukamoto H., Takakura Y., Mine T., Yamamoto T. Photobacterium sp. JT-ISH-224 produces two sialyltransferases, α-/β-galactoside α2,3-sialyltransferase and β-galactoside α2,6-sialyltransferase. J. Biochem. 2008, 143:187-197.
28. Yamamoto T., Nakashizuka M., Kodama H., Kajihara Y., Terada I. Purification and characterization of a marine bacterial β-galactoside α2,6-sialyltransferase from Photobacterium damsela JT0160. J. Biochem. 1996, 120:104-110.
29. Vodkin L.O., Rhodes P.R., Goldberg R.B. cA lectin gene insertion has the structural features of a transposable element. Cell 1983, 34:1023-1031.
30. Waugh D.S. Making the most of affinity tags. Trends Biotechnol. 2005, 23:316-320.
31. Walsh M.K., Swaisgood H.E. An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: expression and bioselective adsorption of streptavidin-β-galactosidase. Biotechnol. Bioeng. 1994, 44:1348-1354.