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Volumn 398, Issue 1, 2010, Pages 32-37

Access to gram scale amounts of functional globular adiponectin from E. coli inclusion bodies by alkaline-shock solubilization

Author keywords

Adiponectin; Alkaline shock; Inclusion bodies; Obesity; Recombinant protein expression

Indexed keywords

ADIPONECTIN; ALKALI;

EID: 77954756849     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.020     Document Type: Article
Times cited : (22)

References (35)
  • 1
    • 0029836585 scopus 로고    scopus 로고
    • Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma
    • Nakano Y., Tobe T., Choi-Miura N.H., Mazda T., Tomita M. Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J. Biochem. (Tokyo) 1996, 120:803-812.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 803-812
    • Nakano, Y.1    Tobe, T.2    Choi-Miura, N.H.3    Mazda, T.4    Tomita, M.5
  • 2
    • 0029980285 scopus 로고    scopus 로고
    • CDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)
    • Maeda K., Okubo K., Shimomura I., Funahashi T., Matsuzawa Y., Matsubara K. CDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1). Biochem. Biophys. Res. Commun. 1996, 221:286-289.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 286-289
    • Maeda, K.1    Okubo, K.2    Shimomura, I.3    Funahashi, T.4    Matsuzawa, Y.5    Matsubara, K.6
  • 3
    • 17544382289 scopus 로고    scopus 로고
    • AdipoQ is a novel adipose-specific gene dysregulated in obesity
    • Hu E., Liang P., Spiegelman B.M. AdipoQ is a novel adipose-specific gene dysregulated in obesity. J. Biol. Chem. 1996, 271:10697-10703.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10697-10703
    • Hu, E.1    Liang, P.2    Spiegelman, B.M.3
  • 4
    • 0028787490 scopus 로고
    • A novel serum protein similar to C1q, produced exclusively in adipocytes
    • Scherer P.E., Williams S., Fogliano M., Baldini G., Lodish H.F. A novel serum protein similar to C1q, produced exclusively in adipocytes. J. Biol. Chem. 1995, 270:26746-26749.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26746-26749
    • Scherer, P.E.1    Williams, S.2    Fogliano, M.3    Baldini, G.4    Lodish, H.F.5
  • 5
    • 0034881391 scopus 로고    scopus 로고
    • The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
    • Berg A.H., Combs T.P., Du X., Brownlee M., Scherer P.E. The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nat. Med. 2001, 7:947-953.
    • (2001) Nat. Med. , vol.7 , pp. 947-953
    • Berg, A.H.1    Combs, T.P.2    Du, X.3    Brownlee, M.4    Scherer, P.E.5
  • 6
    • 0035852760 scopus 로고    scopus 로고
    • Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice
    • Fruebis J., Tsao T.S., Javorschi S., Ebbets-Reed D., Erickson M.R., Yen F.T., Bihain B.E., Lodish H.F. Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc. Natl. Acad. Sci. USA 2001, 98:2005-2010.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2005-2010
    • Fruebis, J.1    Tsao, T.S.2    Javorschi, S.3    Ebbets-Reed, D.4    Erickson, M.R.5    Yen, F.T.6    Bihain, B.E.7    Lodish, H.F.8
  • 11
    • 0347379841 scopus 로고    scopus 로고
    • Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity - different oligomers activate different signal transduction pathways
    • Tsao T.S., Tomas E., Murrey H.E., Hug C., Lee D.H., Ruderman N.B., Heuser J.E., Lodish H.F. Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity - different oligomers activate different signal transduction pathways. J. Biol. Chem. 2003, 278:50810-50817.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50810-50817
    • Tsao, T.S.1    Tomas, E.2    Murrey, H.E.3    Hug, C.4    Lee, D.H.5    Ruderman, N.B.6    Heuser, J.E.7    Lodish, H.F.8
  • 15
    • 62749096761 scopus 로고    scopus 로고
    • Protein kinase CK2 interacts with adiponectin receptor 1 and participates in adiponectin signaling
    • Heiker J.T., Wottawah C.M., Juhl C., Kosel D., Morl K., Beck-Sickinger A.G. Protein kinase CK2 interacts with adiponectin receptor 1 and participates in adiponectin signaling. Cell. Signal. 2009, 21:936-942.
    • (2009) Cell. Signal. , vol.21 , pp. 936-942
    • Heiker, J.T.1    Wottawah, C.M.2    Juhl, C.3    Kosel, D.4    Morl, K.5    Beck-Sickinger, A.G.6
  • 18
    • 0032510463 scopus 로고    scopus 로고
    • The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor
    • Shapiro L., Scherer P.E. The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr. Biol. 1998, 8:335-338.
    • (1998) Curr. Biol. , vol.8 , pp. 335-338
    • Shapiro, L.1    Scherer, P.E.2
  • 20
    • 65349162789 scopus 로고    scopus 로고
    • Adiponectin in health and disease: evaluation of adiponectin-targeted drug development strategies
    • Shetty S., Kusminski C.M., Scherer P.E. Adiponectin in health and disease: evaluation of adiponectin-targeted drug development strategies. Trends Pharmacol. Sci. 2009, 30:234-239.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 234-239
    • Shetty, S.1    Kusminski, C.M.2    Scherer, P.E.3
  • 21
    • 61349193954 scopus 로고    scopus 로고
    • The role of adiponectin in obesity, diabetes, and cardiovascular disease
    • Kawano J., Arora R. The role of adiponectin in obesity, diabetes, and cardiovascular disease. J. Cardiometab. Syndr. 2009, 4:44-49.
    • (2009) J. Cardiometab. Syndr. , vol.4 , pp. 44-49
    • Kawano, J.1    Arora, R.2
  • 23
    • 0037066603 scopus 로고    scopus 로고
    • ACRP30, a new hormone controlling fat and glucose metabolism
    • Tsao T.S., Lodish H.F., Fruebis J. ACRP30, a new hormone controlling fat and glucose metabolism. Eur. J. Pharmacol. 2002, 440:213-221.
    • (2002) Eur. J. Pharmacol. , vol.440 , pp. 213-221
    • Tsao, T.S.1    Lodish, H.F.2    Fruebis, J.3
  • 25
  • 26
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 2005, 41:207-234.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 27
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • Sivashanmugam A., Murray V., Cui C., Zhang Y., Wang J., Li Q. Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci. 2009, 18:936-948.
    • (2009) Protein Sci. , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.3    Zhang, Y.4    Wang, J.5    Li, Q.6
  • 28
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2006
    • Walsh G. Biopharmaceutical benchmarks 2006. Nat. Biotechnol. 2006, 24:769-776.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 769-776
    • Walsh, G.1
  • 29
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 1996, 10:49-56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 30
    • 0027550009 scopus 로고
    • Improved procedure for a high-yield recovery of enzymatically active recombinant calf chymosin from Escherichia coli inclusion bodies
    • Tichy P.J., Kapralek F., Jecmen P. Improved procedure for a high-yield recovery of enzymatically active recombinant calf chymosin from Escherichia coli inclusion bodies. Protein Expr. Purif. 1993, 4:59-63.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 59-63
    • Tichy, P.J.1    Kapralek, F.2    Jecmen, P.3
  • 31
    • 0007577117 scopus 로고    scopus 로고
    • Mechanism of enhancement of prochymosin renaturation by solubilization of inclusion bodies at alkaline pH
    • Zhang Z., Zhang Y., Yang K. Mechanism of enhancement of prochymosin renaturation by solubilization of inclusion bodies at alkaline pH. Sci. China C Life Sci. 1997, 40:169-175.
    • (1997) Sci. China C Life Sci. , vol.40 , pp. 169-175
    • Zhang, Z.1    Zhang, Y.2    Yang, K.3
  • 32
    • 0034534992 scopus 로고    scopus 로고
    • Refolding, structural transition and spermatozoa-binding of recombinant bonnet monkey (Macaca radiata) zona pellucida glycoprotein-C expressed in Escherichia coli
    • Patra A.K., Gahlay G.K., Reddy B.V., Gupta S.K., Panda A.K. Refolding, structural transition and spermatozoa-binding of recombinant bonnet monkey (Macaca radiata) zona pellucida glycoprotein-C expressed in Escherichia coli. Eur. J. Biochem. 2000, 267:7075-7081.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 7075-7081
    • Patra, A.K.1    Gahlay, G.K.2    Reddy, B.V.3    Gupta, S.K.4    Panda, A.K.5
  • 33
    • 55049133746 scopus 로고    scopus 로고
    • Improved solubilization of recombinant human growth hormone inclusion body produced in Escherichia coli
    • Sonoda H., Sugimura A. Improved solubilization of recombinant human growth hormone inclusion body produced in Escherichia coli. Biosci. Biotechnol. Biochem. 2008, 72:2675-2680.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 2675-2680
    • Sonoda, H.1    Sugimura, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.