메뉴 건너뛰기




Volumn 8, Issue 6, 1998, Pages 709-716

Maltose Binding Protein (MBP) Fusion Proteins with Low or No Affinity to Amylose Resins Can Be Single-Step Purified Using a Novel Anti-MBP Monoclonal Antibody

Author keywords

Maltose Binding Protein; Monoclonal Antibody; Protein Purification

Indexed keywords

ABC TRANSPORTER; AMYLOSE; ANION EXCHANGE RESIN; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; GLUCOSE TRANSPORTER; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MALTOSE TRANSPORT SYSTEM, E COLI; MALTOSE-BINDING PROTEIN; MONOCLONAL ANTIBODY; SEPHAROSE;

EID: 0032585349     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (18)
  • 1
    • 0000589382 scopus 로고    scopus 로고
    • Specific binding of the hepatitis B virus preS antigen to an EBV-transformed B-cell line
    • Choi, E. A., Park, J. H., Cho, E. W., Hahm, K. S., and Kim, K. L. (1996) Specific binding of the hepatitis B virus preS antigen to an EBV-transformed B-cell line. Mol. Cells 6, 622-627.
    • (1996) Mol. Cells , vol.6 , pp. 622-627
    • Choi, E.A.1    Park, J.H.2    Cho, E.W.3    Hahm, K.S.4    Kim, K.L.5
  • 2
    • 0029086245 scopus 로고
    • Expression and characterization of branched-chain alpha-ketoacid dehydrogenase kinase from the rat. Is it a histidine-protein kinase?
    • Davie, J. R., Wynn, R. M., Meng, M., Huang, Y. S., Aalund, G., Chuang, D. T., and Lau, K. S. (1995) Expression and characterization of branched-chain alpha-ketoacid dehydrogenase kinase from the rat. Is it a histidine-protein kinase? J. Biol. Chem. 270, 19861-19867.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19861-19867
    • Davie, J.R.1    Wynn, R.M.2    Meng, M.3    Huang, Y.S.4    Aalund, G.5    Chuang, D.T.6    Lau, K.S.7
  • 3
    • 0028866861 scopus 로고
    • Cloning, sequence analysis, overproduction in Escherichia coli and enzymatic characterization of the RNase HI from Mycobacterium smegmatis
    • Dawes, S. S., Crouch, R. J., Morris, S. L., and Mizrahi, V. (1995) Cloning, sequence analysis, overproduction in Escherichia coli and enzymatic characterization of the RNase HI from Mycobacterium smegmatis. Gene 165, 71-75.
    • (1995) Gene , vol.165 , pp. 71-75
    • Dawes, S.S.1    Crouch, R.J.2    Morris, S.L.3    Mizrahi, V.4
  • 4
    • 0025246096 scopus 로고
    • Preparation of monoclonal antibodies
    • Deutscher, M. P. (Ed.), Academic Press, Inc., London
    • Dunbar, B. S. and Skinner, S. M. (1990) Preparation of monoclonal antibodies; in Guide to Protein Purification, Methods in Enzymology, Deutscher, M. P. (Ed.), 182, pp. 670-679, Academic Press, Inc., London.
    • (1990) Guide to Protein Purification, Methods in Enzymology , vol.182 , pp. 670-679
    • Dunbar, B.S.1    Skinner, S.M.2
  • 5
    • 0017990368 scopus 로고
    • Isolation of pure IgG1, IgG2a, and IgG2b immunoglobulins from mouse serum using protein A Sepharose
    • Ey, P. L., Prowse, S. J., and Jenkin, C. R. (1978) Isolation of pure IgG1, IgG2a, and IgG2b immunoglobulins from mouse serum using protein A Sepharose. Biochemistry 15, 429-436.
    • (1978) Biochemistry , vol.15 , pp. 429-436
    • Ey, P.L.1    Prowse, S.J.2    Jenkin, C.R.3
  • 6
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988a) Antibodies: A Laboratory Manual, pp. 27-28, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual , pp. 27-28
    • Harlow, E.1    Lane, D.2
  • 7
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988b) Antibodies: A Laboratory Manual, pp. 354-355, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual , pp. 354-355
    • Harlow, E.1    Lane, D.2
  • 8
    • 0030586874 scopus 로고    scopus 로고
    • Purification and characterization of decorin core protein expressed in Escherichia coli as a maltose-binding protein fusion
    • Hering, T. M., Kollar, J., Huynh, T. D., and Varelas, J. B. (1996) Purification and characterization of decorin core protein expressed in Escherichia coli as a maltose-binding protein fusion. Analyt. Biochem. 240, 98-108.
    • (1996) Analyt. Biochem. , vol.240 , pp. 98-108
    • Hering, T.M.1    Kollar, J.2    Huynh, T.D.3    Varelas, J.B.4
  • 9
    • 0028890251 scopus 로고
    • Hepatitis C virus core protein: Synthesis, affinity purification and immunoreactivity with infected human sera
    • Khanna, A. and Ray, R. (1995) Hepatitis C virus core protein: synthesis, affinity purification and immunoreactivity with infected human sera. Gene 153, 185-189.
    • (1995) Gene , vol.153 , pp. 185-189
    • Khanna, A.1    Ray, R.2
  • 10
    • 0027488492 scopus 로고
    • Induction of T-cell responses by chimeric bacterial proteins expressing several copies of a viral T-cell epitope
    • Lo-Man, R., Martineau, P., Hofnung, M., and Leclerc, C. (1993) Induction of T-cell responses by chimeric bacterial proteins expressing several copies of a viral T-cell epitope. Eur. J. Immunol. 23, 2998-3002.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2998-3002
    • Lo-Man, R.1    Martineau, P.2    Hofnung, M.3    Leclerc, C.4
  • 11
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina, C. V., Riggs, P. D., Grandea, A. G., Slatko, B. E., Moran, L. S., Tagliamonte, J. A., McReynolds, L. A., and di Guan, C. (1988) An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene 74, 365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Di Guan, C.8
  • 12
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
    • Miller, D. M., Olson, J. S., Pflugrath, J. W., and Quiocho, F. A. (1983) Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258, 13665-13672.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13665-13672
    • Miller, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 13
    • 0025212138 scopus 로고
    • Affinity chromatography: General methods
    • Deutscher, M. P. (Ed.), Academic Press, Inc., London
    • Ostrove, S. (1990) Affinity chromatography: General methods; in Guide to Protein Purification, Methods in Enzymology, Deutscher, M. P. (Ed.), 182, pp.357-371, Academic Press, Inc., London.
    • (1990) Guide to Protein Purification, Methods in Enzymology , vol.182 , pp. 357-371
    • Ostrove, S.1
  • 14
    • 0028025473 scopus 로고
    • High level expression of hepatitis B virus preS1 peptide in Escherichia coli
    • Rhyum, S. B., Jin, B. R., Park, H. R., and Hong, H. J. (1994) High level expression of hepatitis B virus preS1 peptide in Escherichia coli. J. Biotech. 36, 221-230.
    • (1994) J. Biotech. , vol.36 , pp. 221-230
    • Rhyum, S.B.1    Jin, B.R.2    Park, H.R.3    Hong, H.J.4
  • 15
    • 14744267241 scopus 로고
    • The functional expression of antibody fragments in Escherichia coli; Improved vectors and a generally applicable purification technique
    • Skerra, A., Pfitzinger, I., and Pluckthun, A. (1991) The functional expression of antibody fragments in Escherichia coli; Improved vectors and a generally applicable purification technique. Bio Technology 9, 273-278.
    • (1991) Bio Technology , vol.9 , pp. 273-278
    • Skerra, A.1    Pfitzinger, I.2    Pluckthun, A.3
  • 16
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith, D. B. and Johnson, K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 17
    • 0029073298 scopus 로고
    • Cloning and expression of mamba toxins
    • Smith, L. A., Olson, M. A., Lafaye, P. J., and Dolly, J. O. (1995) Cloning and expression of mamba toxins. Toxicon 33, 459-474.
    • (1995) Toxicon , vol.33 , pp. 459-474
    • Smith, L.A.1    Olson, M.A.2    Lafaye, P.J.3    Dolly, J.O.4
  • 18
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose-binding or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G.-Y., and Quiocho, F. A. (1991) The 2.3 Å resolution structure of the maltose-binding or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.