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Volumn 48, Issue 1, 2006, Pages 151-159

Refolding, purification, and characterization of human and murine RegIII proteins expressed in Escherichia coli

Author keywords

C type lectins; Carbohydrate binding; Inflammatory bowel disease; Mucosal injury; Regenerating protein family

Indexed keywords

BIOPOLYMER; LECTIN; MANNOSE; PANCREATITIS ASSOCIATED PROTEIN; PANCREATITIS-ASSOCIATED PROTEIN; PROTEIN; RECOMBINANT PROTEIN; REGIII PROTEIN, MOUSE; TUMOR ANTIGEN; TUMOR MARKER;

EID: 33646871553     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.01.014     Document Type: Article
Times cited : (56)

References (33)
  • 4
    • 0033829865 scopus 로고    scopus 로고
    • Identification of genes involved in mucosal defense and inflammation associated with normal enteric bacteria
    • Ogawa H., Fukushima K., Sasaki I., and Matsuno S. Identification of genes involved in mucosal defense and inflammation associated with normal enteric bacteria. Am. J. Physiol. Gastrointest. Liver Physiol. 279 (2000) G492-G499
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279
    • Ogawa, H.1    Fukushima, K.2    Sasaki, I.3    Matsuno, S.4
  • 6
    • 17644393206 scopus 로고    scopus 로고
    • Activation of RegIIIβ/γ and interferon γ expression in the intestinal tract of SCID mice: an innate response to bacterial colonisation of the gut
    • Keilbaugh S.A., Shin M.E., Banchereau R.F., McVay L.D., Boyko N., Artis D., Cebra J.J., and Wu G.D. Activation of RegIIIβ/γ and interferon γ expression in the intestinal tract of SCID mice: an innate response to bacterial colonisation of the gut. Gut 54 (2005) 623-629
    • (2005) Gut , vol.54 , pp. 623-629
    • Keilbaugh, S.A.1    Shin, M.E.2    Banchereau, R.F.3    McVay, L.D.4    Boyko, N.5    Artis, D.6    Cebra, J.J.7    Wu, G.D.8
  • 7
    • 0036840337 scopus 로고    scopus 로고
    • Expression of the regenerating gene family in inflammatory bowel disease mucosa: Reg Iα upregulation, processing, and antiapoptotic activity
    • Dieckgraefe B.K., Crimmins D.L., Landt V., Houchen C., Anant S., Porche-Sorbet R., and Ladenson J.H. Expression of the regenerating gene family in inflammatory bowel disease mucosa: Reg Iα upregulation, processing, and antiapoptotic activity. J. Investig. Med. 50 (2002) 421-434
    • (2002) J. Investig. Med. , vol.50 , pp. 421-434
    • Dieckgraefe, B.K.1    Crimmins, D.L.2    Landt, V.3    Houchen, C.4    Anant, S.5    Porche-Sorbet, R.6    Ladenson, J.H.7
  • 8
    • 0034118415 scopus 로고    scopus 로고
    • High expression of the human hepatocarcinoma-intestine-pancreas/pancreatic-associated protein (HIP/PAP) gene in the mammary gland of lactating transgenic mice. Secretion into the milk and purification of the HIP/PAP lectin
    • Christa L., Pauloin A., Simon M.T., Stinnakre M.G., Fontaine M.L., Delpal S., Ollivier-Bousquet M., Brechot C., and Devinoy E. High expression of the human hepatocarcinoma-intestine-pancreas/pancreatic-associated protein (HIP/PAP) gene in the mammary gland of lactating transgenic mice. Secretion into the milk and purification of the HIP/PAP lectin. Eur. J. Biochem. 267 (2000) 1665-1671
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1665-1671
    • Christa, L.1    Pauloin, A.2    Simon, M.T.3    Stinnakre, M.G.4    Fontaine, M.L.5    Delpal, S.6    Ollivier-Bousquet, M.7    Brechot, C.8    Devinoy, E.9
  • 9
    • 0027958753 scopus 로고
    • The human HIP gene, overexpressed in primary liver cancer encodes for a C-type carbohydrate binding protein with lactose binding activity
    • Christa L., Felin M., Morali O., Simon M.T., Lasserre C., Brechot C., and Seve A.P. The human HIP gene, overexpressed in primary liver cancer encodes for a C-type carbohydrate binding protein with lactose binding activity. FEBS Lett. 337 (1994) 114-118
    • (1994) FEBS Lett. , vol.337 , pp. 114-118
    • Christa, L.1    Felin, M.2    Morali, O.3    Simon, M.T.4    Lasserre, C.5    Brechot, C.6    Seve, A.P.7
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley A., Whitmore L., and Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18 (2002) 211-212
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 13
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Bohm G., Muhr R., and Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5 (1992) 191-195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Bohm, G.1    Muhr, R.2    Jaenicke, R.3
  • 14
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama N., and Woody R.W. Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242 (1994) 497-507
    • (1994) J. Mol. Biol. , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 15
    • 0142011590 scopus 로고    scopus 로고
    • Structure-function analysis of C-type animal lectins
    • Taylor M.E., and Drickamer K. Structure-function analysis of C-type animal lectins. Methods Enzymol. 363 (2003) 3-16
    • (2003) Methods Enzymol. , vol.363 , pp. 3-16
    • Taylor, M.E.1    Drickamer, K.2
  • 17
    • 0034958310 scopus 로고    scopus 로고
    • High-level expression of three members of the murine angiogenin family in Escherichia coli and purification of the recombinant proteins
    • Holloway D.E., Hares M.C., Shapiro R., Subramanian V., and Acharya K.R. High-level expression of three members of the murine angiogenin family in Escherichia coli and purification of the recombinant proteins. Protein Expr. Purif. 22 (2001) 307-317
    • (2001) Protein Expr. Purif. , vol.22 , pp. 307-317
    • Holloway, D.E.1    Hares, M.C.2    Shapiro, R.3    Subramanian, V.4    Acharya, K.R.5
  • 18
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • De Bernardez Clark E., Schwarz E., and Rudolph R. Inhibition of aggregation side reactions during in vitro protein folding. Methods Enzymol. 309 (1999) 217-236
    • (1999) Methods Enzymol. , vol.309 , pp. 217-236
    • De Bernardez Clark, E.1    Schwarz, E.2    Rudolph, R.3
  • 20
    • 0038394449 scopus 로고    scopus 로고
    • Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells
    • Stambach N.S., and Taylor M.E. Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells. Glycobiology 13 (2003) 401-410
    • (2003) Glycobiology , vol.13 , pp. 401-410
    • Stambach, N.S.1    Taylor, M.E.2
  • 21
    • 0030874378 scopus 로고    scopus 로고
    • Adsorption of pulmonary surfactant protein D to phospholipid monolayers at the air-water interface
    • Taneva S., Voelker D.R., and Keough K.M. Adsorption of pulmonary surfactant protein D to phospholipid monolayers at the air-water interface. Biochemistry 36 (1997) 8173-8179
    • (1997) Biochemistry , vol.36 , pp. 8173-8179
    • Taneva, S.1    Voelker, D.R.2    Keough, K.M.3
  • 22
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis W.I., and Drickamer K. Trimeric structure of a C-type mannose-binding protein. Structure 2 (1994) 1227-1240
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 24
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K., Molgaard A., Gupta R., and Brunak S. Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 15 (2005) 153-164
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 28
    • 0033286202 scopus 로고    scopus 로고
    • The Reg gene family and Reg proteins: with special attention to the regeneration of pancreatic β-cells
    • Okamoto H. The Reg gene family and Reg proteins: with special attention to the regeneration of pancreatic β-cells. J. Hepatobiliary Pancreat. Surg. 6 (1999) 254-262
    • (1999) J. Hepatobiliary Pancreat. Surg. , vol.6 , pp. 254-262
    • Okamoto, H.1
  • 29
    • 0142245698 scopus 로고    scopus 로고
    • Expression of a novel regenerating gene product, Reg IV, by high density fermentation in Pichia pastoris: production, purification, and characterization
    • Li A., Crimmins D.L., Luo Q., Hartupee J., Landt Y., Ladenson J.H., Wilson D., Anant S., and Dieckgraefe B.K. Expression of a novel regenerating gene product, Reg IV, by high density fermentation in Pichia pastoris: production, purification, and characterization. Protein Expr. Purif. 31 (2003) 197-206
    • (2003) Protein Expr. Purif. , vol.31 , pp. 197-206
    • Li, A.1    Crimmins, D.L.2    Luo, Q.3    Hartupee, J.4    Landt, Y.5    Ladenson, J.H.6    Wilson, D.7    Anant, S.8    Dieckgraefe, B.K.9
  • 30
    • 0142121656 scopus 로고    scopus 로고
    • High-level expression of porcine liver cytochrome P-450 reductase catalytic domain in Escherichia coli by modulating the predicted local secondary structure of mRNA
    • Kimura S., and Iyanagi T. High-level expression of porcine liver cytochrome P-450 reductase catalytic domain in Escherichia coli by modulating the predicted local secondary structure of mRNA. J. Biochem. (Tokyo) 134 (2003) 403-413
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 403-413
    • Kimura, S.1    Iyanagi, T.2
  • 31
    • 0038348638 scopus 로고    scopus 로고
    • Role of the mannose-binding lectin in innate immunity
    • Ezekowitz R.A. Role of the mannose-binding lectin in innate immunity. J. Infect. Dis. 187 Suppl. 2 (2003) S335-S339
    • (2003) J. Infect. Dis. , vol.187 , Issue.SUPPL. 2
    • Ezekowitz, R.A.1
  • 32
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis W.I., Drickamer K., and Hendrickson W.A. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360 (1992) 127-134
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 33
    • 0022993935 scopus 로고
    • Immunocytochemical localization of pancreatic stone protein in the human digestive tract
    • Lechene de la Porte P., de Caro A., Lafont H., and Sarles H. Immunocytochemical localization of pancreatic stone protein in the human digestive tract. Pancreas 1 (1986) 301-308
    • (1986) Pancreas , vol.1 , pp. 301-308
    • Lechene de la Porte, P.1    de Caro, A.2    Lafont, H.3    Sarles, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.