메뉴 건너뛰기




Volumn 359, Issue 1-2, 2010, Pages 21-27

IgM characterization directly performed in crude culture supernatants by a new simple electrophoretic method

Author keywords

IgM; IgM electrophoresis; Isoform distribution; Quality profiling; Quantification of IgM

Indexed keywords

FLUORESCENT DYE; IMMUNOGLOBULIN FRAGMENT; IMMUNOGLOBULIN M; POLYMER; PROTEIN; SYPRO RUBY DYE; UNCLASSIFIED DRUG;

EID: 77954382830     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2010.05.003     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 23844468114 scopus 로고    scopus 로고
    • Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin
    • Arnold J., Wormald M., Suter D., Radcliffe C., Harvey D., Dwek R., Rudd P., Sim R. Human serum IgM glycosylation: identification of glycoforms that can bind to mannan-binding lectin. J. Biol. Chem. 2005, 280:29080.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29080
    • Arnold, J.1    Wormald, M.2    Suter, D.3    Radcliffe, C.4    Harvey, D.5    Dwek, R.6    Rudd, P.7    Sim, R.8
  • 3
    • 0021334790 scopus 로고
    • A modified gel filtration technique producing an unusual exclusion volume of IgM: a simple way of preparing monoclonal IgM
    • Bouvet J., Pires R., Pillot J. A modified gel filtration technique producing an unusual exclusion volume of IgM: a simple way of preparing monoclonal IgM. J. Immunol. Meth. 1984, 66:305.
    • (1984) J. Immunol. Meth. , vol.66 , pp. 305
    • Bouvet, J.1    Pires, R.2    Pillot, J.3
  • 4
    • 0028200169 scopus 로고
    • Mechanism and subcellular localization of secretory IgM polymer assembly
    • Brewer J., Randall T., Parkhouse R., Corley R. Mechanism and subcellular localization of secretory IgM polymer assembly. J. Biol. Chem. 1994, 269:17338.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17338
    • Brewer, J.1    Randall, T.2    Parkhouse, R.3    Corley, R.4
  • 5
    • 18544404283 scopus 로고    scopus 로고
    • Natural IgM antibodies and immunosurveillance mechanisms against epithelial cancer cells in humans
    • Brändlein S., Pohle T., Ruoff N., Wozniak E., Müller-Hermelink H., Vollmers H. Natural IgM antibodies and immunosurveillance mechanisms against epithelial cancer cells in humans. Cancer Res. 2003, 63:7995.
    • (2003) Cancer Res. , vol.63 , pp. 7995
    • Brändlein, S.1    Pohle, T.2    Ruoff, N.3    Wozniak, E.4    Müller-Hermelink, H.5    Vollmers, H.6
  • 6
    • 3042781291 scopus 로고    scopus 로고
    • Natural IgM antibodies, the ignored weapons in tumour immunity
    • Brändlein S., Vollmers H. Natural IgM antibodies, the ignored weapons in tumour immunity. Histol. Histopathol. 2004, 19:897.
    • (2004) Histol. Histopathol. , vol.19 , pp. 897
    • Brändlein, S.1    Vollmers, H.2
  • 7
    • 0030909919 scopus 로고    scopus 로고
    • Stringent thiol-mediated retention in B lymphocytes and Xenopus oocytes correlates with inefficient IgM polymerization
    • Carelli S., Ceriotti A., Sitia R. Stringent thiol-mediated retention in B lymphocytes and Xenopus oocytes correlates with inefficient IgM polymerization. Eur. J. Immunol. 1997, 27:1283.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1283
    • Carelli, S.1    Ceriotti, A.2    Sitia, R.3
  • 8
    • 34247557067 scopus 로고    scopus 로고
    • Incomplete assembly of IgA2m(2) in Chinese hamster ovary cells
    • Chintalacharuvu K., Gurbaxani B., Morrison S. Incomplete assembly of IgA2m(2) in Chinese hamster ovary cells. Mol. Immunol. 2007, 44:3445.
    • (2007) Mol. Immunol. , vol.44 , pp. 3445
    • Chintalacharuvu, K.1    Gurbaxani, B.2    Morrison, S.3
  • 9
    • 0022558482 scopus 로고
    • Tandem purification of IgM monoclonal antibodies from mouse ascites fluids by anion-exchange and gel fast protein liquid chromatography
    • Clezardin P., Bougro G., McGregor J. Tandem purification of IgM monoclonal antibodies from mouse ascites fluids by anion-exchange and gel fast protein liquid chromatography. J. Chromatogr. 1986, 354:425.
    • (1986) J. Chromatogr. , vol.354 , pp. 425
    • Clezardin, P.1    Bougro, G.2    McGregor, J.3
  • 10
    • 0036086544 scopus 로고    scopus 로고
    • Differential activation of human and guinea pig complement by pentameric and hexameric IgM
    • Collins C., Tsui F., Shulman M. Differential activation of human and guinea pig complement by pentameric and hexameric IgM. Eur. J. Immunol. 2002, 32:1802.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1802
    • Collins, C.1    Tsui, F.2    Shulman, M.3
  • 11
    • 0024436948 scopus 로고
    • Intermolecular disulfide bonding in IgM: effects of replacing cysteine residues in the mu heavy chain
    • Davis A., Roux K., Pursey J., Shulman M. Intermolecular disulfide bonding in IgM: effects of replacing cysteine residues in the mu heavy chain. EMBO J. 1989, 8:2519.
    • (1989) EMBO J. , vol.8 , pp. 2519
    • Davis, A.1    Roux, K.2    Pursey, J.3    Shulman, M.4
  • 13
    • 0032531976 scopus 로고    scopus 로고
    • Production of IgM hexamers by normal and autoimmune B cells: implications for the physiologic role of hexameric IgM
    • Hughey C., Brewer J., Colosia A., Rosse W., Corley R. Production of IgM hexamers by normal and autoimmune B cells: implications for the physiologic role of hexameric IgM. J. Immunol. 1998, 161:4091.
    • (1998) J. Immunol. , vol.161 , pp. 4091
    • Hughey, C.1    Brewer, J.2    Colosia, A.3    Rosse, W.4    Corley, R.5
  • 15
    • 0036024975 scopus 로고    scopus 로고
    • Blue Native electrophoresis to study mitochondrial and other protein complexes
    • Nijtmans L., Henderson N., Holt I. Blue Native electrophoresis to study mitochondrial and other protein complexes. Methods 2002, 26:327.
    • (2002) Methods , vol.26 , pp. 327
    • Nijtmans, L.1    Henderson, N.2    Holt, I.3
  • 16
    • 0033485791 scopus 로고    scopus 로고
    • The contribution of ER quality control to the biologic functions of secretory IgM
    • Reddy P., Corley R. The contribution of ER quality control to the biologic functions of secretory IgM. Immunol. Today 1999, 20:582.
    • (1999) Immunol. Today , vol.20 , pp. 582
    • Reddy, P.1    Corley, R.2
  • 17
    • 0035371858 scopus 로고    scopus 로고
    • Biotinylation of protein complexes may lead to aggregation as well as to loss of subunits as revealed by Blue Native PAGE
    • Schamel W. Biotinylation of protein complexes may lead to aggregation as well as to loss of subunits as revealed by Blue Native PAGE. J. Immunol. Meth. 2001, 252:171.
    • (2001) J. Immunol. Meth. , vol.252 , pp. 171
    • Schamel, W.1
  • 19
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger H., Cramer W., von Jagow G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 1994, 217:220.
    • (1994) Anal. Biochem. , vol.217 , pp. 220
    • Schägger, H.1    Cramer, W.2    von Jagow, G.3
  • 20
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H., von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199:223.
    • (1991) Anal. Biochem. , vol.199 , pp. 223
    • Schägger, H.1    von Jagow, G.2
  • 24
    • 33747352549 scopus 로고    scopus 로고
    • Natural IgM antibodies: the orphaned molecules in immune surveillance
    • Vollmers H., Brändlein S. Natural IgM antibodies: the orphaned molecules in immune surveillance. Adv. Drug Deliv. Rev. 2006, 58:755.
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , pp. 755
    • Vollmers, H.1    Brändlein, S.2
  • 25
    • 0038219368 scopus 로고    scopus 로고
    • Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins
    • Warren C., Krzesinski P., Greaser M. Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins. Electrophoresis 2003, 24:1695.
    • (2003) Electrophoresis , vol.24 , pp. 1695
    • Warren, C.1    Krzesinski, P.2    Greaser, M.3
  • 27
    • 0032526642 scopus 로고    scopus 로고
    • Structural and functional analysis of J chain-deficient IgM
    • Wiersma E., Collins C., Fazel S., Shulman M. Structural and functional analysis of J chain-deficient IgM. J. Immunol. 1998, 160:5979.
    • (1998) J. Immunol. , vol.160 , pp. 5979
    • Wiersma, E.1    Collins, C.2    Fazel, S.3    Shulman, M.4
  • 28
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clear-native PAGE
    • Wittig I., Schägger H. Advantages and limitations of clear-native PAGE. Proteomics 2005, 5:4338.
    • (2005) Proteomics , vol.5 , pp. 4338
    • Wittig, I.1    Schägger, H.2
  • 30
    • 0037147623 scopus 로고    scopus 로고
    • Inactivation and conformational changes of lactate dehydrogenase from porcine heart in sodium dodecyl sulfate solutions
    • Zheng Y., Meng F., Chen B., Wang X. Inactivation and conformational changes of lactate dehydrogenase from porcine heart in sodium dodecyl sulfate solutions. Int. J. Biol. Macromol. 2002, 31:97.
    • (2002) Int. J. Biol. Macromol. , vol.31 , pp. 97
    • Zheng, Y.1    Meng, F.2    Chen, B.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.