메뉴 건너뛰기




Volumn 311, Issue 1-2, 2006, Pages 153-163

Determination of human transferrin concentrations in mouse models of neisserial infection

Author keywords

Human transferrin; Mouse model; Neisseria meningitidis

Indexed keywords

IRON BINDING PROTEIN; MONOCLONAL ANTIBODY; TRANSFERRIN;

EID: 33646109833     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2006.01.016     Document Type: Article
Times cited : (7)

References (28)
  • 1
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen P., and Listowsky I. Iron transport and storage proteins. Annu. Rev. Biochem. 49 (1980) 357
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 357
    • Aisen, P.1    Listowsky, I.2
  • 2
    • 0027303190 scopus 로고
    • Comparison of transferrin sequences from different species
    • Baldwin G.S. Comparison of transferrin sequences from different species. Comp. Biochem. Physiol., B 106 (1993) 203
    • (1993) Comp. Biochem. Physiol., B , vol.106 , pp. 203
    • Baldwin, G.S.1
  • 3
    • 0037046282 scopus 로고    scopus 로고
    • Both transferrin binding proteins are virulence factors in Actinobacillus pleuropneumoniae serotype 7 infections
    • Baltes N., Hennig-Pauka I., and Gerlach G.F. Both transferrin binding proteins are virulence factors in Actinobacillus pleuropneumoniae serotype 7 infections. FEMS Microbiol. Lett. 209 (2002) 283
    • (2002) FEMS Microbiol. Lett. , vol.209 , pp. 283
    • Baltes, N.1    Hennig-Pauka, I.2    Gerlach, G.F.3
  • 4
    • 12244310166 scopus 로고    scopus 로고
    • Brain iron uptake in hypotransferrinemic mice: influence of systemic iron status
    • Beard J.L., Wiesinger J.A., Li N., and Connor J.R. Brain iron uptake in hypotransferrinemic mice: influence of systemic iron status. J. Neurosci. Res. 79 (2005) 254
    • (2005) J. Neurosci. Res. , vol.79 , pp. 254
    • Beard, J.L.1    Wiesinger, J.A.2    Li, N.3    Connor, J.R.4
  • 6
    • 0017990368 scopus 로고
    • Isolation of pure IgG1, IgG2a, IgG2b, immunoglobulins from mouse serum using protein A-sepharose
    • Ey P.L., Prowse S.J., and Jenkin C.R. Isolation of pure IgG1, IgG2a, IgG2b, immunoglobulins from mouse serum using protein A-sepharose. Immunochemistry 15 (1978) 429
    • (1978) Immunochemistry , vol.15 , pp. 429
    • Ey, P.L.1    Prowse, S.J.2    Jenkin, C.R.3
  • 8
    • 0031451545 scopus 로고    scopus 로고
    • The relation between chemically measured total iron/binding capacity concentrations and immunologically measured transferrin concentrations in human serum
    • Gambino R., Desvarieux E., Orth M., Matan H., Ackattupathil T., Lijoi E., Wimmer C., Bower J., and Gunter E. The relation between chemically measured total iron/binding capacity concentrations and immunologically measured transferrin concentrations in human serum. Clin. Chem. 43 (1997) 2408
    • (1997) Clin. Chem. , vol.43 , pp. 2408
    • Gambino, R.1    Desvarieux, E.2    Orth, M.3    Matan, H.4    Ackattupathil, T.5    Lijoi, E.6    Wimmer, C.7    Bower, J.8    Gunter, E.9
  • 9
    • 0032486130 scopus 로고    scopus 로고
    • The nature of ligand-induced conformational change in transferrin in solution. An investigation using X-ray scattering, XAFS and site-directed mutants
    • Grossmann G., Crawley J.B., Strange R.W., Patel K.J., Murphy L.M., Neu M., Evans R.W., and Hasnain S.S. The nature of ligand-induced conformational change in transferrin in solution. An investigation using X-ray scattering, XAFS and site-directed mutants. J. Mol. Biol. 279 (1998) 461
    • (1998) J. Mol. Biol. , vol.279 , pp. 461
    • Grossmann, G.1    Crawley, J.B.2    Strange, R.W.3    Patel, K.J.4    Murphy, L.M.5    Neu, M.6    Evans, R.W.7    Hasnain, S.S.8
  • 10
    • 33646092973 scopus 로고    scopus 로고
    • Harlow, E., Lane, D., 1988. Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory, NY, p. 340.
  • 11
    • 0019360750 scopus 로고
    • Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin
    • Holbein B.E. Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin. Infect. Immun. 34 (1981) 120
    • (1981) Infect. Immun. , vol.34 , pp. 120
    • Holbein, B.E.1
  • 13
    • 0032491199 scopus 로고    scopus 로고
    • Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin
    • Jeffrey P.D., Bewley M.C., MacGillivray R.T., and Mason A.B. Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin. Biochemistry 37 (1998) 13978
    • (1998) Biochemistry , vol.37 , pp. 13978
    • Jeffrey, P.D.1    Bewley, M.C.2    MacGillivray, R.T.3    Mason, A.B.4
  • 14
    • 0018726056 scopus 로고
    • A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines
    • Kearney J.F., Radbruch A., Liesegang B., and Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J. Immunol. 123 (1979) 1548
    • (1979) J. Immunol. , vol.123 , pp. 1548
    • Kearney, J.F.1    Radbruch, A.2    Liesegang, B.3    Rajewsky, K.4
  • 16
    • 0014670422 scopus 로고
    • Factors affecting the synthesis of transferrin by rat tissue slice
    • Morgan E.H. Factors affecting the synthesis of transferrin by rat tissue slice. J. Biol. Chem. 244 (1969) 4193
    • (1969) J. Biol. Chem. , vol.244 , pp. 4193
    • Morgan, E.H.1
  • 17
    • 0032917738 scopus 로고    scopus 로고
    • Epitope Analysis of a Prostate-specific Antigen (PSA) C-Terminal-specific monoclonal antibody and new aspects for the discrepancy between equimolar and skewed PSA assays
    • Nagasaki H., Watanabe M., Komatsu N., and Kaneko T. Epitope Analysis of a Prostate-specific Antigen (PSA) C-Terminal-specific monoclonal antibody and new aspects for the discrepancy between equimolar and skewed PSA assays. Clin. Chem. 45 (1999) 486
    • (1999) Clin. Chem. , vol.45 , pp. 486
    • Nagasaki, H.1    Watanabe, M.2    Komatsu, N.3    Kaneko, T.4
  • 18
    • 0032851445 scopus 로고    scopus 로고
    • A mouse model utilising human transferrin to study protection against Neisseria meningitidis serogroup B induced by outer membrane vesicle vaccination
    • Oftung F., Lovik M., Andersen S.R., Froholm L.O., and Bjune G. A mouse model utilising human transferrin to study protection against Neisseria meningitidis serogroup B induced by outer membrane vesicle vaccination. FEMS Immunol. Med. Microbiol. 26 (1999) 75
    • (1999) FEMS Immunol. Med. Microbiol. , vol.26 , pp. 75
    • Oftung, F.1    Lovik, M.2    Andersen, S.R.3    Froholm, L.O.4    Bjune, G.5
  • 19
    • 0028157937 scopus 로고
    • Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature
    • O'Shannessy D.J. Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature. Curr. Opin. Biotechnol. 5 (1994) 65
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 65
    • O'Shannessy, D.J.1
  • 23
    • 0024323936 scopus 로고
    • Comparison of the abilities of different protein sources of iron to enhance Neisseria meningitidis infection in mice
    • Schryvers A.B., and Gonzales G.C. Comparison of the abilities of different protein sources of iron to enhance Neisseria meningitidis infection in mice. Infect. Immun. 57 (1989) 2425
    • (1989) Infect. Immun. , vol.57 , pp. 2425
    • Schryvers, A.B.1    Gonzales, G.C.2
  • 24
    • 0025212523 scopus 로고
    • Receptors for transferrin in pathogenic bacteria are specific for the host's protein
    • Schryvers A.B., and Gonzales G.C. Receptors for transferrin in pathogenic bacteria are specific for the host's protein. Can. J. Microbiol. 36 (1990) 145
    • (1990) Can. J. Microbiol. , vol.36 , pp. 145
    • Schryvers, A.B.1    Gonzales, G.C.2
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets procedure and some applications
    • Towbin H.T., Staehelin T., and Gordon J. Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets procedure and some applications. Proc. Natl. Acad. Sci. 76 (1979) 4350
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 4350
    • Towbin, H.T.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 0037379542 scopus 로고    scopus 로고
    • Development and evaluation of an improved mouse model of meningoccocal colonization
    • Yi K., Stephens D.S., and Stojiljkovic I. Development and evaluation of an improved mouse model of meningoccocal colonization. Infect. Immun. 71 (2003) 1849
    • (2003) Infect. Immun. , vol.71 , pp. 1849
    • Yi, K.1    Stephens, D.S.2    Stojiljkovic, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.