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2003 | 08 | 3 |

Tytuł artykułu

Concanavalin A-agarose removes mannan impurities from an extracellularly expressed Pichia pastoris recombinant protein

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Pichia pastoris secretes few native proteins. However, the more than 1 g 1-1 of extracellularly expressed mannan interfered with the purification of our extracellularly expressed, non-glycosylated recombinant protein. Concanavalin A-agarose removed more than 95% of the unwanted mannan as monitored by phenol reaction. A 13C-based NMR assay confirmed this improvement. Concanavalin A-agarose can assist the purification of extracellular expressed, non-glycosylated proteins from yeasts.

Wydawca

-

Rocznik

Tom

08

Numer

3

Opis fizyczny

p.783-792,fig.

Twórcy

autor
  • Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland
autor
autor

Bibliografia

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  • 5.Ecamilla-Trevino, L.L., Viader-Salvadó, J.M., Barrera-Saldana, H.A. and Guerrero-Olazarán, M. Biosynthesis and secretion of recombinant human growth hormone in Pichia pastoris. Biotechnol. Lett. 22 (2000) 109-114.
  • 6.Lee, K.Y. and Do, S.I. Differential and cell-type specific microheterogeneity of high mannose-type Asn-linked oligosaccharides of human transferrin receptor. Mol. Cells 12 (2001) 239-243.
  • 7.Roy, I., Sharma, S. and Gupta, M.N. Separation of an isoenzyme of polyphenol oxidase from Duranta plumieri by expanded bed chromatography. Prot. Expr. Purif. 24 (2002) 181-187.
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  • 11.Hodge, J.E. and Hofreiter, B.T. Determination of reducing sugars and carbohydrates, in: Methods in Carbohydrate Chemistry, (Whistler, R.L. and Wolfrom, M.W., Eds.) Vol. 1, Academic Press, N.Y., (1962) 380-399.
  • 12.Bradford, M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254.
  • 13.Palczewska, M., Groves, P., Batta, G., Heise, B. and Kuźnicki, J. Calretinin and calbindin D28k have different domain organizations. Prot. Sci. 12 (2003) 180-184.
  • 14.Palczewska, M., Groves, P., Ambrus, A., Kaleta, A., Kövér, K.E., Batta, G. and Kuźnicki, J. Structural and biochemical characterization of neuronal calretinin domain I-II (residues 1-100): comparison to homologous calbindin D28k domain I-II (residues 1-93). Eur. J. Biochem. 268 (2001) 6229-6237.
  • 15.Vinogradov, E., Petersen, B.O. and Duus, J.O. Isolation and characterization of non-labeled and l3C-labeled mannans from Pichia pastoris yeast. Carbohydr. Res. 325 (2000) 216-221.
  • 16.Denton, H., Smith, M., Husi, H., Uhrin, D., Barlow, P.N., Batt, C.A. and Sawyer, L. Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pastoris. Prot. Expr. Purif. 14 (1998) 97-103.
  • 17.Kennedy, J.F. and Pagliuca, G. Oligosaccharides. In: Carbohydrate analysis: a practical approach (Chaplin, M.F. and Kennedy, J.F., Eds.) Oxford University Press, New York, (1994) chapter 2.
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  • 19.Morgan, W.D., Birdsall, B., Frenkiel, T.A., Gradwell, M.G., Burghaus, P.A., Syed, S.E., Uthaipibull, C., Holder, A.A. and Feeney, J. Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1. J. Mol. Biol. 289 (1999) 113-122.
  • 20.Karpusas, M., Cachero, T.G., Qian, F., Boriack-Sjodin, A., Mullen, C., Strauch, K., Hsu, Y.M. and Kalled, S.L. Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes. J. Mol. Biol. 315 (2002) 1145-1154.
  • 21.Chirgadze, D.Y., Hepple, J.P., Zhou, H., Byrd, R.A., Blundell, T.L. and Gherardi, E. Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding. Nat. Struct. Biol. 6 (1999) 72-79.
  • 22.Pickford, A.R., Smith, S.P., Staunton, D., Boyd, J. and Campbell, I.D. The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J. 20 (2001) 1519-1529.
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Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-b9cfb597-82c2-4f08-a05c-640ab2eb7412
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