Characterization of the large size aggregation of Hepatitis B virus surface antigen (HBsAg) formed in ultrafiltration process

Process Biochemistry

Volumn 42, Issue 3, 2007, Pages 315-319

  Li, Yan ^a,b   Bi, Jingxiu ^a   Zhou, Weibin ^a   Huang, Yongdong ^a,b   Sun, Lijing ^a,b   Zeng, An Ping ^c   Ma, Guanghui ^a   Su, Zhiguo ^a  

^a INSTITUTE OF PROCESS ENGINEERING   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c HAMBURG UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

Hepatitis B surface antigen (HBsAg); Membrane ultrafiltration; Protein aggregation

Indexed keywords

ANTIGENS; BIOASSAY; LIGHT SCATTERING; MOLECULAR SPECTROSCOPY; MOLECULAR STRUCTURE; ULTRAFILTRATION;

HEPATITIS B SURFACE ANTIGEN (HBSAG); MEMBRANE ULTRAFILTRATION; PROTEIN AGGREGATION;

BACTERIA;

HEPATITIS B VIRUS;

EID: 33847368496     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2006.08.016     Document Type: Article

References (22)

1. Deml L., Schirmbeck R., Reimann J., Wolf H., and Wagner R. Purification and characterization of hepatitis B virus surface antigen particles produced in Drosophila schneider-2 cells. J Virol. Methods 79 (1999) 205-217
2. Youn B.W., and Samanta H. Purification and characterization of pre-S-containing hepatitis B surface antigens produced in recombinant mammalian cell culture. Vaccine 7 (1989) 60-68
3. Junior S.S.M., Vianna C.O.A., Ennes I., Gomes S.A., Freire M.S., Silva E.D., et al. Simple immunoaffinity method to purify recombinant hepatitis B surface antigen secreted by transfected mammalian cells. J. Chromatogr. B 787 (2003) 303-311
4. Belew M., Mei Y., Li B., Berglof J., and Janson J.C. Purification of recombinant hepatitis B virus surface antigen produced by transformed Chinese Hamster Ovary (CHO) cell line grown in culture. Bioseparation 1 (1991) 397-408
5. Wijnendaele V, Frans, Simonet, Guy. Method for the isolation and purification of hepatitis B surface antigen using polysorbate. US Patent 4,649,192; 1987.
6. Yamazaki, Shigeko. Process for purifying recombinant hepatitis antigens. US Patent 5,011,915; 1991.
7. Friedman, Arthur, Lehman, Dale E, McAleer, William J, Schaefer, Ted F, Scolnick, Edward M, Wampler D, Eugene. Immunogenic HBsAg derived from transformed yeast. US Patent 4,707,542; 1987.
8. Method for obtaining recombinant surface antigen of hepatitis B virus (HEP B). 480525EP; 1991.
9. Huisman I.H., Prádanos P., and Hernández A. The effect of protein-protein and protein-membrane interactions on membrane fouling in ultrafiltration. J. Membr. Sci. 179 (2000) 79-90
10. Maruyama T., Katoh S., Nakajima M., and Nabetani H. Mechanism of bovine serum albumin aggregation during ultrafiltration. Biotechnol. Bioeng. 75 (2001) 233-238
11. Fields G.B., Alonso D.O.V., Stiger D., and Dill K.A. Theory for the aggregation of proteins and copolymers. J. Phys. Chem. 96 (1992) 3974-3981
12. Speed M.A., Wang D.I.C., and King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body. Nat. Biotechnol. 14 (1996) 1283-1287
13. McAllister C., Karymov M.A., Kawano Y., Lushnikov A.Y., Mikheikin A., Vladimir Uversky N., et al. Protein interactions and misfolding analyzed by AFM force spectroscopy. J. Mol. Biol. 354 (2005) 1028-1104
14. Palacio L., Ho C.C., Prádanos P., Hernández A., and Zydney A.L. Fouling with protein mixtures in microfiltration: BSA-lysozyme and BSA-pepsin. J. Membr. Sci. 222 (2003) 41-51
15. Gavilanes F., González-Ros J.M., and Peterson D.L. Structure of hepatitis B surface antigen. J. Biol. Chem. 257 (1982) 7770-7777
16. Ganem D., and Varmus H.E. The molecular biology of the hepatitis B viruses. Rev. Biochem. 56 (1987) 651-693
17. Satoh O., Umeda M., Imai H., Tunoo H., and Inoue K. Lipid composition of hepatitis B virus surface antigen particles and the particles producing human hepatoma cell lines. J. Lipid Res. 31 (1990) 1293-1300
18. Diminsky D., Schirmbeck R., Reimann J., and Barenholz Y. Comparison between hepatitis B surface antigen (HBsAg) particles derived from mammalian cells (CHO) and yeast cells (Hansenula polymorpha): composition, structure and immunogenicity. Vaccine 15 (1997) 637-647
19. Dreesman G.R., Hollinger F.B., Suriano J.R., Fujioka R.S., Brunchwig J.P., and Melnick J. Biophysical and biochemical heterogeneity of purified hepatitis B antigen. J. Virol. 10 (1972) 469-476
20. 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
21. Diminsky D., Moav N., Gorecki M., and Barenholz Y. Physical, chemical and immunological stability of CHO-derived hepatictis B surface antigen (HBsAg) particles. Vaccine 18 (2000) 3-17
22. Zhou W.B., Bi J.X., Janson J.C., Li Y., Huang Y.D., Zhang Y., et al. Molecular characterization of recombinant hepatitis B surface antigen from Chinese hamster ovary and Hansenula polymorpha cells by high-performance size exclusion chromatography and multi-angle laser light scattering. J. Chromatogr. B 838 (2006) 71-77