메뉴 건너뛰기




Volumn 361, Issue 1-2, 2008, Pages 92-98

Butyroyl-arginine as a potent virus inactivation agent

Author keywords

Arginine; Butyroyl arginine; Influenza virus; Sendai virus; Virus inactivation

Indexed keywords

ARGININE; ARGININE DERIVATIVE; BUTYROYLARGININE; CITRIC ACID; RECOMBINANT ANTIBODY; RECOMBINANT PROTEIN; VIRUS HEMAGGLUTININ; VIRUS PROTEIN;

EID: 47949084283     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2008.05.020     Document Type: Article
Times cited : (22)

References (37)
  • 1
    • 33847217198 scopus 로고    scopus 로고
    • Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects
    • Arakawa T., Ejima D., et al. Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. Biophys. Chem. 127 (2007) 1-8
    • (2007) Biophys. Chem. , vol.127 , pp. 1-8
    • Arakawa, T.1    Ejima, D.2
  • 2
    • 33748588923 scopus 로고    scopus 로고
    • Aggregation suppression of protein by arginine
    • Arakawa T., Kita Y., et al. Aggregation suppression of protein by arginine. Protein Pept. Lett. 13 (2006) 921-927
    • (2006) Protein Pept. Lett. , vol.13 , pp. 921-927
    • Arakawa, T.1    Kita, Y.2
  • 3
    • 3142537435 scopus 로고    scopus 로고
    • Elution of antibodies from a Protein-A column by aqueous arginine solutions
    • Arakawa T., Philo J.S., et al. Elution of antibodies from a Protein-A column by aqueous arginine solutions. Protein Expr. Purif. 36 (2004) 244-248
    • (2004) Protein Expr. Purif. , vol.36 , pp. 244-248
    • Arakawa, T.1    Philo, J.S.2
  • 4
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation
    • Arakawa T., and Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304 (2003) 148-152
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 5
    • 0037420743 scopus 로고    scopus 로고
    • Bracketed generic inactivation of rodent retroviruses by low pH treatment for monoclonal antibodies and recombinant proteins
    • Brorson K., Krejci S., et al. Bracketed generic inactivation of rodent retroviruses by low pH treatment for monoclonal antibodies and recombinant proteins. Biotechnol. Bioeng. 82 (2003) 321-329
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 321-329
    • Brorson, K.1    Krejci, S.2
  • 6
    • 16444380194 scopus 로고    scopus 로고
    • Current and future approaches to ensure the viral safety of biopharmaceuticals
    • Brorson K., and Norling L. Current and future approaches to ensure the viral safety of biopharmaceuticals. Dev. Biol. 118 (2004) 17-29
    • (2004) Dev. Biol. , vol.118 , pp. 17-29
    • Brorson, K.1    Norling, L.2
  • 7
    • 33749253824 scopus 로고    scopus 로고
    • Purification of intravenous immunoglobulin G from human plasma-aspects of yield and virus safety
    • Buchacher A., and Iberer G. Purification of intravenous immunoglobulin G from human plasma-aspects of yield and virus safety. Biotechnol. J. 1 (2006) 148-163
    • (2006) Biotechnol. J. , vol.1 , pp. 148-163
    • Buchacher, A.1    Iberer, G.2
  • 8
    • 33847059215 scopus 로고    scopus 로고
    • Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies
    • Ejima D., Tsumoto K., et al. Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies. Proteins 66 (2007) 954-962
    • (2007) Proteins , vol.66 , pp. 954-962
    • Ejima, D.1    Tsumoto, K.2
  • 9
    • 25444492027 scopus 로고    scopus 로고
    • Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography
    • Ejima D., Yumioka R., et al. Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography. Anal. Biochem. 345 (2005) 250-257
    • (2005) Anal. Biochem. , vol.345 , pp. 250-257
    • Ejima, D.1    Yumioka, R.2
  • 10
    • 25844440975 scopus 로고    scopus 로고
    • The clearance of viruses and transmissible spongiform encephalopathy agents from biologicals
    • Farshid M., Taffs R.E., et al. The clearance of viruses and transmissible spongiform encephalopathy agents from biologicals. Curr. Opin. Biotechnol. 16 (2005) 561-567
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 561-567
    • Farshid, M.1    Taffs, R.E.2
  • 11
    • 13844272399 scopus 로고    scopus 로고
    • Membrane-permeable arginine-rich peptides and the translocation mechanism
    • Futaki S. Membrane-permeable arginine-rich peptides and the translocation mechanism. Adv. Drug Deliv. Rev. 57 (2005) 547-558
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 547-558
    • Futaki, S.1
  • 12
    • 0037378389 scopus 로고    scopus 로고
    • The likelihood of aggregation during protein renaturation can be assesses using the second virial coefficient
    • Ho J.G., Middelberg A.P., et al. The likelihood of aggregation during protein renaturation can be assesses using the second virial coefficient. Protein Sci. 12 (2003) 708-716
    • (2003) Protein Sci. , vol.12 , pp. 708-716
    • Ho, J.G.1    Middelberg, A.P.2
  • 14
    • 0032924058 scopus 로고    scopus 로고
    • A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions
    • Kaushik J.K., and Bhat R. A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions. Protein Sci. 8 (1999) 222-233
    • (1999) Protein Sci. , vol.8 , pp. 222-233
    • Kaushik, J.K.1    Bhat, R.2
  • 15
    • 0028618410 scopus 로고
    • Contribution of the surface free energy perturbation to protein-solvent interactions
    • Kita Y., Arakawa T., et al. Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry 33 (1994) 15178-15189
    • (1994) Biochemistry , vol.33 , pp. 15178-15189
    • Kita, Y.1    Arakawa, T.2
  • 16
    • 0035201806 scopus 로고    scopus 로고
    • Suppression of apoptotic and necrotic cell death by poliovirus
    • Koyama A.H., Irie H., et al. Suppression of apoptotic and necrotic cell death by poliovirus. J. Gen. Virol. 8 (2001) 2965-2972
    • (2001) J. Gen. Virol. , vol.8 , pp. 2965-2972
    • Koyama, A.H.1    Irie, H.2
  • 17
    • 0038666142 scopus 로고    scopus 로고
    • Virus multiplication and induction of apoptosis by Sendai virus: role of C proteins
    • Koyama A.H., Irie H., et al. Virus multiplication and induction of apoptosis by Sendai virus: role of C proteins. Microbes Infection 5 (2003) 373-378
    • (2003) Microbes Infection , vol.5 , pp. 373-378
    • Koyama, A.H.1    Irie, H.2
  • 18
    • 0023190313 scopus 로고
    • The mode of entry of herpes simplex virus type 1 into Vero cells
    • Koyama A.H., and Uchida T. The mode of entry of herpes simplex virus type 1 into Vero cells. Microbiol. Immunol. 31 (1987) 123-130
    • (1987) Microbiol. Immunol. , vol.31 , pp. 123-130
    • Koyama, A.H.1    Uchida, T.2
  • 19
    • 0024374807 scopus 로고
    • The effect of ammonium chloride on the multiplication of herpes simplex virus type 1 in Vero cells
    • Koyama A.H., and Uchida T. The effect of ammonium chloride on the multiplication of herpes simplex virus type 1 in Vero cells. Virus Res. 13 (1989) 271-282
    • (1989) Virus Res. , vol.13 , pp. 271-282
    • Koyama, A.H.1    Uchida, T.2
  • 20
    • 0033124625 scopus 로고    scopus 로고
    • Influenza virus overcomes apoptosis by rapid multiplication
    • Kurokawa M., Koyama A.H., et al. Influenza virus overcomes apoptosis by rapid multiplication. Int. J. Mol. Med. 3 (1999) 527-530
    • (1999) Int. J. Mol. Med. , vol.3 , pp. 527-530
    • Kurokawa, M.1    Koyama, A.H.2
  • 21
    • 0030040794 scopus 로고    scopus 로고
    • On the role of surface tension in the stabilization of globular proteins
    • Lin T.Y., and Timasheff S.N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 5 (1996) 372-381
    • (1996) Protein Sci. , vol.5 , pp. 372-381
    • Lin, T.Y.1    Timasheff, S.N.2
  • 22
    • 0028605960 scopus 로고
    • Large increase in thermal stability of the CH2 domain of rabbit IgG after acid treatment as evidenced by differential scanning calorimetry
    • Martsef S.P., Kravchuk Z.I., et al. Large increase in thermal stability of the CH2 domain of rabbit IgG after acid treatment as evidenced by differential scanning calorimetry. Immunol. Lett. 43 (1994) 149-152
    • (1994) Immunol. Lett. , vol.43 , pp. 149-152
    • Martsef, S.P.1    Kravchuk, Z.I.2
  • 23
    • 0028916303 scopus 로고
    • Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH-induced state
    • Martsef S.P., Kravxhuk Z.I., et al. Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH-induced state. FEBS Lett. 361 (1995) 173-175
    • (1995) FEBS Lett. , vol.361 , pp. 173-175
    • Martsef, S.P.1    Kravxhuk, Z.I.2
  • 24
    • 0030828879 scopus 로고    scopus 로고
    • Comparison of two different methods for inactivation of viruses in serum
    • Preuss T., Kamstrup S., et al. Comparison of two different methods for inactivation of viruses in serum. Clin. Diagn. Lab. Immunol. 4 (1997) 504-508
    • (1997) Clin. Diagn. Lab. Immunol. , vol.4 , pp. 504-508
    • Preuss, T.1    Kamstrup, S.2
  • 25
    • 15244343628 scopus 로고    scopus 로고
    • l-Arginine increases the solbility of unfolded species of hen egg lysozyme
    • Reddy K.R.C., Lilie H., et al. l-Arginine increases the solbility of unfolded species of hen egg lysozyme. Protein Sci. 14 (2005) 929-935
    • (2005) Protein Sci. , vol.14 , pp. 929-935
    • Reddy, K.R.C.1    Lilie, H.2
  • 26
    • 35248888115 scopus 로고    scopus 로고
    • Virus inactivation by protein denaturants used in affinity chromatography
    • Roberts P.L., and Lloyd D. Virus inactivation by protein denaturants used in affinity chromatography. Biologicals 35 (2007) 343-347
    • (2007) Biologicals , vol.35 , pp. 343-347
    • Roberts, P.L.1    Lloyd, D.2
  • 27
    • 4644240799 scopus 로고    scopus 로고
    • Real time quantitative PCR as a method to evaluate xenotropic murine leukemia virus removal during pharmaceutical protein purification
    • Shi L., Chen Q., et al. Real time quantitative PCR as a method to evaluate xenotropic murine leukemia virus removal during pharmaceutical protein purification. Biotechnol. Bioeng. 87 (2004) 884-896
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 884-896
    • Shi, L.1    Chen, Q.2
  • 28
    • 0036774673 scopus 로고    scopus 로고
    • Biophysical effect of amino acids on the prevention of protein aggregation
    • Shiraki K., Kudou M., et al. Biophysical effect of amino acids on the prevention of protein aggregation. J. Biochem. (Tokyo) 132 (2002) 591-595
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 591-595
    • Shiraki, K.1    Kudou, M.2
  • 29
    • 24944581330 scopus 로고    scopus 로고
    • Review: why is arginine effective in suppressing aggregation?
    • Tsumoto K., Ejima D., et al. Review: why is arginine effective in suppressing aggregation?. Protein Pept. Lett. 12 (2005) 613-619
    • (2005) Protein Pept. Lett. , vol.12 , pp. 613-619
    • Tsumoto, K.1    Ejima, D.2
  • 30
    • 34249742157 scopus 로고    scopus 로고
    • Arginine improves protein elution in hydrophobic interaction chromatography. The cases of human interleukin-6 and activin-A
    • Tsumoto K., Ejima D., et al. Arginine improves protein elution in hydrophobic interaction chromatography. The cases of human interleukin-6 and activin-A. J. Chromatogr. A. 1154 (2007) 81-86
    • (2007) J. Chromatogr. A. , vol.1154 , pp. 81-86
    • Tsumoto, K.1    Ejima, D.2
  • 31
    • 0344495223 scopus 로고    scopus 로고
    • Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine
    • Tsumoto K., Umetsu M., et al. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun. 312 (2003) 1383-1386
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1383-1386
    • Tsumoto, K.1    Umetsu, M.2
  • 32
    • 5444228298 scopus 로고    scopus 로고
    • Role of arginine in protein refolding, solubilization, and purification
    • Tsumoto K., Umetsu M., et al. Role of arginine in protein refolding, solubilization, and purification. Biotechnol. Prog. 20 (2004) 1301-1308
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1301-1308
    • Tsumoto, K.1    Umetsu, M.2
  • 33
    • 12844284637 scopus 로고    scopus 로고
    • Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by L-arginine
    • Umetsu M., Tsumoto K., Nitta S., et al. Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by L-arginine. Biochem. Biophys. Res. Commun. 328 (2005) 189-197
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 189-197
    • Umetsu, M.1    Tsumoto, K.2    Nitta, S.3
  • 34
    • 33846362237 scopus 로고    scopus 로고
    • Antiviral effect of octyl gallate against DNA and RNA viruses
    • Uozaki M., Yamasaki H., et al. Antiviral effect of octyl gallate against DNA and RNA viruses. Antiviral Res. 73 (2007) 85-91
    • (2007) Antiviral Res. , vol.73 , pp. 85-91
    • Uozaki, M.1    Yamasaki, H.2
  • 35
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein.
    • Vermeer A.W.P., and Norde W. The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophys. J. 78 (2000) 394-404
    • (2000) Biophys. J. , vol.78 , pp. 394-404
    • Vermeer, A.W.P.1    Norde, W.2
  • 36
    • 47949113253 scopus 로고    scopus 로고
    • Arginine facilitates inactivation of enveloped viruses
    • Yamasaki H., Tsujimoto K., et al. Arginine facilitates inactivation of enveloped viruses. J Pharm Sci 97 (2008) 3067-3073
    • (2008) J Pharm Sci , vol.97 , pp. 3067-3073
    • Yamasaki, H.1    Tsujimoto, K.2
  • 37
    • 34247871300 scopus 로고    scopus 로고
    • Antiviral effect of octyl gallate against influenza and other RNA viruses
    • Yamasaki H., Uozaki M., et al. Antiviral effect of octyl gallate against influenza and other RNA viruses. Int. J. Mol. Med. 19 (2007) 685-688
    • (2007) Int. J. Mol. Med. , vol.19 , pp. 685-688
    • Yamasaki, H.1    Uozaki, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.