Co-operative thermal inactivation of herpes simplex virus and influenza virus by arginine and NaCl

International Journal of Pharmaceutics

Volumn 366, Issue 1-2, 2009, Pages 99-102

  Utsunomiya, Hirotoshi ^a   Ichinose, Masao ^a   Tsujimoto, Kazuko ^a   Katsuyama, Yukiko ^a   Yamasaki, Hisashi ^a   Koyama, A Hajime ^a   Ejima, Daisuke ^b   Arakawa, Tsutomu ^c  

^a WAKAYAMA MEDICAL UNIVERSITY   (Japan)

^b AJINOMOTO CO INC   (Japan)

^c ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

Arginine; HSV 1; Influenza virus; Temperature dependence; Virus inactivation

Indexed keywords

ARGININE; PHOSPHATE BUFFERED SALINE; SODIUM CHLORIDE;

ANIMAL CELL; ARTICLE; CONCENTRATION RESPONSE; HERPES SIMPLEX VIRUS 1; INFLUENZA VIRUS A; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE DEPENDENCE; VIRUS INACTIVATION;

ANIMALS; ANTIVIRAL AGENTS; ARGININE; CELL LINE; CERCOPITHECUS AETHIOPS; DOGS; DOSE-RESPONSE RELATIONSHIP, DRUG; HERPESVIRUS 1, HUMAN; INFLUENZA A VIRUS; OSMOLAR CONCENTRATION; SODIUM CHLORIDE; TEMPERATURE; VERO CELLS;

EID: 57849084750     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2008.09.012     Document Type: Article

References (28)

1. Arakawa T., Kita Y., et al. Solubility enhancement of gluten and organic compounds by arginine. Int. J. Pharm. 355 (2008) 220-223
2. Arakawa T., and Timasheff S.N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 21 (1982) 6545-6552
3. Arakawa T., and Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refdolign, but suppress aggregation. Biochem. Biophys. Res. Commun. 304 (2003) 148-152
4. Arakawa T., Philo J.S., et al. Elution of antibodies from a Protein-A column by aqueous arginine solutions. Protein Exp. Purif. 36 (2005) 244-248
5. Arora D., and Khanna N. Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J. Biotechnol. 52 (1996) 127-133
6. 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
7. Evengard B., Ehrnst A., et al. Effect of heat on extracted HIV vira; infectivity and antibody using the filter paper technique of blood sampling. AIDS 3 (1989) 591-595
8. Gouda M.D., Singh S.A., et al. Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives. J. Biol. Chem. 278 (2003) 24324-24333
9. Graham D.A., and Staples C. Biophysical properties of salmonid alphaviruses: influence of temperature and pH on virus survival. J. Fish Dis. 30 (2007) 533-543
10. Hirano A., Arakawa T., et al. Arginine increases the solubility of coumarin: comparison with salting-in and salting-out additives. J. Biochem. 144 (2008) 363-369
11. Ho J.G., Middleberg A.P., et al. The likelihood of aggregation during protein renaturation can be assessed using the second viral coefficient. Protein Sci. 12 (2003) 708-716
12. Katsuyama, Y., Yamasaki, H., et al., 2008. Butyroyl-arginine as a potent virus inactivation agent.
13. 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
14. Kurokawa M., Koyama A.H., et al. Influenza virus overcomes apoptosis by rapid multiplication. Int. J. Mol. Med. 3 (1999) 527-530
15. Liu X.Q., Yang X.Q., et al. On-column refolding and purification of transglutaminase from Streptomyces fradiae expressed as inclusion bodies in Escherichia coli. Protein Exp. Purif. 51 (2007) 179-186
16. Liu Y.D., Zhang G.F., et al. Identification of an oxidative refolding intermediate of recombinant consensus interferon from inclusion bodies and design of a two-state strategy to promote correct disulfide-bond formation. Biotechnol. Appl. Biochem. 48 (2007) 189-198
17. Norwak T., Gregersen J.P., et al. Viral safety of human immunoglobulins: efficient inactivation of hepatitis C and other human pathogenic viruses by the manufacturing procedure. J. Med. Virol. 36 (1992) 209-216
18. Ross P.D., Finlayson J.S., et al. Thermal stability of human albumin measured by differential scanning calorimetry. II. Effects of isomers of N-acetyltryptopahanate and tryptophanate, pH, reheating, and dimerization. Vox Sang. 47 (1984) 19-27
19. Saboury A.A., Atri M.S., et al. Effects of calcium binding on the strutcure and stability of human growth hormone. Int. J. Biol. Macromol. 36 (2005) 305-309
20. Smales C.M., Pepper D.S., et al. Protein modification during antiviral heat bioprocessing. Biotechnol. Bioeng. 67 (2000) 177-188
21. Suenaga M., Ohmae H., et al. Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregates. Biotechnol. Appl. Biochem. 28 (1998) 119-124
22. Swayne D.E., and Beck J.R. Heat inactivation of avian influenza and Newcastle disease viruses in egg products. Avian Pathol. 33 (2004) 512-518
23. Tomasula P.M., Kozempel M.F., et al. Thermal inactivation of foot-and-mouth disease virus in milk using high-temperature, short-time pasteurization. J. Dairy Sci. 90 (2007) 3203-3211
24. 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
25. 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
26. Umetsu M., Tsumoto K., et al. Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by l-arginine. Biochem. Biophys. Res. Commun. 328 (2005) 189-197
27. Yamasaki H., Tsujimoto K., et al. Arginine facilitates inactivation of enveloped viruses. J. Pharm. Sci. 97 (2008) 3067-3073
28. Yu M.W., and Finlayson J.S. Stabilization of human albumin by caprylate and acetyltryptophanate. Vox Sang. 47 (1984) 28-40