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Volumn 248, Issue 2, 1997, Pages 602-614

Mass determination, subunit organization and control of oligomerization states of keyhole limpet hemocyanin (KLH)

Author keywords

Hemocyanin; Keyhold limpet; Megathura crenulata; Mollusca; Quaternary structure

Indexed keywords

KEYHOLE LIMPET HEMOCYANIN;

EID: 0030886451     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00602.x     Document Type: Article
Times cited : (47)

References (68)
  • 2
    • 0017844298 scopus 로고
    • Functional and structural properties of Murex fulvescens hemocyanin: Isolation of two different subunits required for reassociation of a molluscan hemocyanin
    • Brouwer, M., Ryan, M., Bonaventura, J. & Bonaventura, C. (1978) Functional and structural properties of Murex fulvescens hemocyanin: isolation of two different subunits required for reassociation of a molluscan hemocyanin, Biochemistry 17, 2810-2815.
    • (1978) Biochemistry , vol.17 , pp. 2810-2815
    • Brouwer, M.1    Ryan, M.2    Bonaventura, J.3    Bonaventura, C.4
  • 3
    • 0028925266 scopus 로고
    • IL-12 inhibits IL-4 synthesis in keyhole limpel hemocyanin-primed CD4 + T cells through an affect on antigen-presenting cells
    • DeKruyff, R. H., Fang, Y., Wolf, S. F. & Umetsu, D. T. (1995) IL-12 inhibits IL-4 synthesis in keyhole limpel hemocyanin-primed CD4 + T cells through an affect on antigen-presenting cells, J. Immunol. 15, 2578-2587.
    • (1995) J. Immunol. , vol.15 , pp. 2578-2587
    • DeKruyff, R.H.1    Fang, Y.2    Wolf, S.F.3    Umetsu, D.T.4
  • 4
    • 0029586905 scopus 로고
    • Three-dimensional structure of keyhole limpet hemocyanin by cryoelectron microscopy and angular reconstitution
    • Dube, P., Orlova, E. V., Zemlin, F., van Heel, M. Harris, J. R. & Markl, J. (1995) Three-dimensional structure of keyhole limpet hemocyanin by cryoelectron microscopy and angular reconstitution, J. Struct. Biol. 115, 226-232.
    • (1995) J. Struct. Biol. , vol.115 , pp. 226-232
    • Dube, P.1    Orlova, E.V.2    Zemlin, F.3    Van Heel, M.4    Harris, J.R.5    Markl, J.6
  • 5
    • 0018197443 scopus 로고
    • Molecular mass determination by scanning transmission electron microscopy
    • Engel, A. (1978) Molecular mass determination by scanning transmission electron microscopy, Ultramicroscopy 3, 273-281.
    • (1978) Ultramicroscopy , vol.3 , pp. 273-281
    • Engel, A.1
  • 6
    • 0020158294 scopus 로고
    • Mass mapping of a protein complex with the scanning electron microscope
    • Engel, A., Baumeister, W. & Saxton, W. O. (1982) Mass mapping of a protein complex with the scanning electron microscope, Proc. Natl Acad. Sci. USA 79, 4050-4054.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 4050-4054
    • Engel, A.1    Baumeister, W.2    Saxton, W.O.3
  • 7
    • 0024226569 scopus 로고
    • Processing of quantitative scanning transmission electron micrographs
    • Engel, A. & Reichelt, R. (1988) Processing of quantitative scanning transmission electron micrographs, Scanning Microsc. Suppl. 2, 285-293.
    • (1988) Scanning Microsc. , Issue.2 SUPPL. , pp. 285-293
    • Engel, A.1    Reichelt, R.2
  • 9
    • 0009729509 scopus 로고
    • Identification, separation and characterization of the hemocyanin components of Helix aspersa
    • Gielens, C., De Sadeleer, J., Preaux, G. & Lontie, R. (1987) Identification, separation and characterization of the hemocyanin components of Helix aspersa, Comp. Biochem. Physiol. B 88, 181-186.
    • (1987) Comp. Biochem. Physiol. B , vol.88 , pp. 181-186
    • Gielens, C.1    De Sadeleer, J.2    Preaux, G.3    Lontie, R.4
  • 10
    • 0028930004 scopus 로고
    • Limited proteolysis of the haemocyanin of the gastropod Pila leopoldvillensis. Isolation and characterization of fragments
    • Gielens, C., Declerq, L. & Preaux, G. (1995) Limited proteolysis of the haemocyanin of the gastropod Pila leopoldvillensis. Isolation and characterization of fragments, Comp. Biochem. Physiol. B 110, 565-575.
    • (1995) Comp. Biochem. Physiol. B , vol.110 , pp. 565-575
    • Gielens, C.1    Declerq, L.2    Preaux, G.3
  • 11
    • 0023215210 scopus 로고
    • Schistosoma mansoni shares a protective carbohydrate epitope with keyhole limpet hemocyanin
    • Grzych, J.-M., Dissous, C., Capron, M., Torres, S., Lambert, P.-H. & Capron, A. (1987) Schistosoma mansoni shares a protective carbohydrate epitope with keyhole limpet hemocyanin, J. Exp. Med. 165, 865-878.
    • (1987) J. Exp. Med. , vol.165 , pp. 865-878
    • Grzych, J.-M.1    Dissous, C.2    Capron, M.3    Torres, S.4    Lambert, P.-H.5    Capron, A.6
  • 12
    • 0024942004 scopus 로고
    • Scanning transmission electron microscopic study of molluscan hemocyanin in various aggregation states: Comparison with light scattering molecular masses
    • Hamilton, M. G., Herskovits, T. T., Furcinitti, P. S. & Wall, J. S. (1989) Scanning transmission electron microscopic study of molluscan hemocyanin in various aggregation states: comparison with light scattering molecular masses, J. Ultrastruct. Mol. Struct. Res. 102, 221-228.
    • (1989) J. Ultrastruct. Mol. Struct. Res. , vol.102 , pp. 221-228
    • Hamilton, M.G.1    Herskovits, T.T.2    Furcinitti, P.S.3    Wall, J.S.4
  • 13
    • 44049120182 scopus 로고
    • Two-dimensional crystallization, transmission electron microscopy and image processing of keyhole limpet hemocyanin (KLH)
    • Harris, J. R., Cejka, Z., Wegener-Strake, A., Gebauer, W. & Markl, J. (1992) Two-dimensional crystallization, transmission electron microscopy and image processing of keyhole limpet hemocyanin (KLH), Micron. Microsc. Acta 23, 287-301.
    • (1992) Micron. Microsc. Acta , vol.23 , pp. 287-301
    • Harris, J.R.1    Cejka, Z.2    Wegener-Strake, A.3    Gebauer, W.4    Markl, J.5
  • 14
    • 0027723370 scopus 로고
    • Immunoelectron microscopy of hemocyanin from the keyhole limpet (Megathura crenulata): A parallel subunit model
    • Harris, J. R., Gebauer, W. & Markl, J. (1993) Immunoelectron microscopy of hemocyanin from the keyhole limpet (Megathura crenulata): a parallel subunit model, J. Struct. Biol. 111, 96-104.
    • (1993) J. Struct. Biol. , vol.111 , pp. 96-104
    • Harris, J.R.1    Gebauer, W.2    Markl, J.3
  • 15
    • 0001383317 scopus 로고
    • Keyhole limpet haemocyanin (KLH): Purification of intact KLH1 through selective dissociation of KLH2
    • Harris, J. R., Gebauer, W., Söhngen, S. & Markl, J. (1995a) Keyhole limpet haemocyanin (KLH): Purification of intact KLH1 through selective dissociation of KLH2, Micron 26, 201-212.
    • (1995) Micron , vol.26 , pp. 201-212
    • Harris, J.R.1    Gebauer, W.2    Söhngen, S.3    Markl, J.4
  • 16
    • 0029159273 scopus 로고
    • Keyhole limpet hemocyanin (KLH): Negative staining in the presence of trehalose
    • Harris, J. R., Gebauer, W. & Markl, J. (1995b) Keyhole limpet hemocyanin (KLH): Negative staining in the presence of trehalose, Micron 26, 25-33.
    • (1995) Micron , vol.26 , pp. 25-33
    • Harris, J.R.1    Gebauer, W.2    Markl, J.3
  • 17
    • 0031080434 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH) I: Reassociation from Immucothel followed by separation of KLH1 and KLH2
    • Harris, J. R., Gebauer, W., Guderian, F. U. M. & Markl, J. (1997a) Keyhole limpet hemocyanin (KLH) I: reassociation from Immucothel followed by separation of KLH1 and KLH2, Micron 28, 31-41.
    • (1997) Micron , vol.28 , pp. 31-41
    • Harris, J.R.1    Gebauer, W.2    Guderian, F.U.M.3    Markl, J.4
  • 18
    • 0031080603 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH) II: Characteristic reassociation properties of purified KLH1 and KLH2
    • Harris, J. R., Gebauer, W., Söhngen, S. M., Nermut, M. V. & Markl, J. (1997b) Keyhole limpet hemocyanin (KLH) II: characteristic reassociation properties of purified KLH1 and KLH2, Micron 28, 43-56.
    • (1997) Micron , vol.28 , pp. 43-56
    • Harris, J.R.1    Gebauer, W.2    Söhngen, S.M.3    Nermut, M.V.4    Markl, J.5
  • 19
    • 0000035583 scopus 로고
    • Separation and absorption spectra of α and β hemocyanin of Helix pomatia
    • Heirwegh, K., Borginon, H. & Lontie, R. (1961) Separation and absorption spectra of α and β hemocyanin of Helix pomatia, Biochim. Biophys. Acta 48, 517-526.
    • (1961) Biochim. Biophys. Acta , vol.48 , pp. 517-526
    • Heirwegh, K.1    Borginon, H.2    Lontie, R.3
  • 21
    • 0023056476 scopus 로고
    • Light scattering investigation of the subunit structure and dissociation of octopoda hemocyanins
    • Herskovits, T. T. & Villanueva, G. B. (1986) Light scattering investigation of the subunit structure and dissociation of octopoda hemocyanins, Biochemistry 25, 931-939.
    • (1986) Biochemistry , vol.25 , pp. 931-939
    • Herskovits, T.T.1    Villanueva, G.B.2
  • 22
    • 0024248001 scopus 로고
    • Recent aspects of the subunit organisation and dissociation of molecular masses of proteins by disc gel electrophoresis
    • Herskovits, T. T. (1988) Recent aspects of the subunit organisation and dissociation of molecular masses of proteins by disc gel electrophoresis, Comp. Biochem. Physiol. B 91, 597-611.
    • (1988) Comp. Biochem. Physiol. B , vol.91 , pp. 597-611
    • Herskovits, T.T.1
  • 23
    • 0024808881 scopus 로고
    • Subunit structure and higher order assembly of the hemocyanin of the Melongenidae family: Melongena corona (Gmelin), Busycon canaliculatum (Linné), B. carica (Gmelin), B. contrarium (Conrad), and B. spiratum (Lamarck)
    • Herskovits, T. T., Blake, P. A., Gonzalez, J. A., Hamilton, M. G. & Wall, J. S. (1989) Subunit structure and higher order assembly of the hemocyanin of the Melongenidae family: Melongena corona (Gmelin), Busycon canaliculatum (Linné), B. carica (Gmelin), B. contrarium (Conrad), and B. spiratum (Lamarck), Comp. Biochem. Physiol. B 94, 415-421.
    • (1989) Comp. Biochem. Physiol. B , vol.94 , pp. 415-421
    • Herskovits, T.T.1    Blake, P.A.2    Gonzalez, J.A.3    Hamilton, M.G.4    Wall, J.S.5
  • 25
    • 0028926040 scopus 로고
    • The hemocyanin of the Californian black sea hare, Aplysia vaccinia Winkler
    • Herskovits, T. T., Edwards, M. D. & Hamilton, M. G. (1995) The hemocyanin of the Californian black sea hare, Aplysia vaccinia Winkler, Comp. Biochem. Physiol. B 110, 515-521.
    • (1995) Comp. Biochem. Physiol. B , vol.110 , pp. 515-521
    • Herskovits, T.T.1    Edwards, M.D.2    Hamilton, M.G.3
  • 26
    • 0027279837 scopus 로고
    • Structural properties of Rapana thomasiana Grosse hemocyanin: Isolation, characterization and N-terminal amino acid sequence of two different dissociation products
    • Idakieva, K., Severov, S., Svendsen, I., Genov, N., Stoeva, S., Beltramini, M., Tognon, G., Di Muro, P. & Salvato, B. (1993) Structural properties of Rapana thomasiana Grosse hemocyanin: isolation, characterization and N-terminal amino acid sequence of two different dissociation products, Comp. Biochem. Physiol. B 106, 53-59.
    • (1993) Comp. Biochem. Physiol. B , vol.106 , pp. 53-59
    • Idakieva, K.1    Severov, S.2    Svendsen, I.3    Genov, N.4    Stoeva, S.5    Beltramini, M.6    Tognon, G.7    Di Muro, P.8    Salvato, B.9
  • 27
    • 0344909403 scopus 로고
    • Subunit structure of hemocyanin from the gastropod Levantina hierosolima
    • Ilan, E., Avissar, I., Banin, D. & Daniel, E. (1986) Subunit structure of hemocyanin from the gastropod Levantina hierosolima, Biochemistry 25, 4994-4999.
    • (1986) Biochemistry , vol.25 , pp. 4994-4999
    • Ilan, E.1    Avissar, I.2    Banin, D.3    Daniel, E.4
  • 28
    • 0028285354 scopus 로고
    • Specific immunization using keyhole limpet hemocyanin-ganglioside conjugates
    • Jennemann, R., Gnewuch, C., Boisslet, S., Bauer, B. L. & Wiegandt, H. (1994) Specific immunization using keyhole limpet hemocyanin-ganglioside conjugates, J. Biochem. (Tokyo) 115, 1047-1052.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 1047-1052
    • Jennemann, R.1    Gnewuch, C.2    Boisslet, S.3    Bauer, B.L.4    Wiegandt, H.5
  • 29
    • 0023934840 scopus 로고
    • Immunotherapy in bladder cancer with keyhole limpet hemocyanin - A randomized study
    • Jurincic, C. D., Engelmann, U., Gasch, J. & Klippel, K.-F. (1988) Immunotherapy in bladder cancer with keyhole limpet hemocyanin - a randomized study, J. Urol. 139, 723-726.
    • (1988) J. Urol. , vol.139 , pp. 723-726
    • Jurincic, C.D.1    Engelmann, U.2    Gasch, J.3    Klippel, K.-F.4
  • 30
    • 0000910851 scopus 로고
    • On the quaternary structure of HTH, the hemocyanin from the abalone Haliotis tuberculata
    • Keller, H., Söhngen, S. M. & Markl, J. (1995) On the quaternary structure of HTH, the hemocyanin from the abalone Haliotis tuberculata, Verh. Dtsch. Zool. Ges 88, 109.
    • (1995) Verh. Dtsch. Zool. Ges , vol.88 , pp. 109
    • Keller, H.1    Söhngen, S.M.2    Markl, J.3
  • 31
    • 0014688989 scopus 로고
    • Structure and properties of hemocyanins. VI. Association-dissociation behavior of Helix pomatia hemocyanin
    • Konings, W. N., Siezen, R. J. & Gruber, M. (1969) Structure and properties of hemocyanins. VI. Association-dissociation behavior of Helix pomatia hemocyanin, Biochim. Biophys. Acta 194, 376-385.
    • (1969) Biochim. Biophys. Acta , vol.194 , pp. 376-385
    • Konings, W.N.1    Siezen, R.J.2    Gruber, M.3
  • 32
    • 0015838530 scopus 로고
    • Crossed-line immunoelectrophoresis
    • Kroll, J. (1973) Crossed-line immunoelectrophoresis, Scand. J. Immunol. 2 (Suppl. 1), 79-81.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.1 SUPPL. , pp. 79-81
    • Kroll, J.1
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0028990445 scopus 로고
    • Three-dimensional reconstruction of the αD and βC-hemocyanins of Helix pomatia from frozen-hydrated specimens
    • Lambert, O., Boisset, N., Taveau, J.-C., Preaux, G. & Lamy, J. N. (1995) Three-dimensional reconstruction of the αD and βC-hemocyanins of Helix pomatia from frozen-hydrated specimens, J. Mol. Biol. 248, 431-448.
    • (1995) J. Mol. Biol. , vol.248 , pp. 431-448
    • Lambert, O.1    Boisset, N.2    Taveau, J.-C.3    Preaux, G.4    Lamy, J.N.5
  • 37
    • 0027258004 scopus 로고
    • Further approaches to the quaternary structure of Octopus hemocyanin: A model based on immunoelectron microscopy and image processing
    • Lamy, J., Gielens, C., Lambert, O., Taveau, J. C., Motta, G., Loncke, P., De Geest, N., Preaux, G. & Lamy, J. (1993) Further approaches to the quaternary structure of Octopus hemocyanin: a model based on immunoelectron microscopy and image processing, Arch. Biochem. Biophys. 305, 17-29.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 17-29
    • Lamy, J.1    Gielens, C.2    Lambert, O.3    Taveau, J.C.4    Motta, G.5    Loncke, P.6    De Geest, N.7    Preaux, G.8    Lamy, J.9
  • 38
    • 84908813060 scopus 로고
    • Evidence for two types of polypeptide chains in the hemocyanin of Buccinum undatum
    • Lips, D., Gielen, C., Preaux, G. & Lontie, R. (1981) Evidence for two types of polypeptide chains in the hemocyanin of Buccinum undatum, Arch. Int. Physiol. Biochem. 90, B128.
    • (1981) Arch. Int. Physiol. Biochem. , vol.90
    • Lips, D.1    Gielen, C.2    Preaux, G.3    Lontie, R.4
  • 39
    • 0000453895 scopus 로고
    • Subunit-specific monoclonal antibodies to tarantula hemocyanin, and a common epitope shared with calliphorin
    • Markl, J. & Winter, S. (1989) Subunit-specific monoclonal antibodies to tarantula hemocyanin, and a common epitope shared with calliphorin, J. Comp. Physiol. B 159, 139-151.
    • (1989) J. Comp. Physiol. B , vol.159 , pp. 139-151
    • Markl, J.1    Winter, S.2
  • 40
    • 0000222758 scopus 로고
    • Molecular structure of the arthropod hemocyanins
    • Markl, J. & Decker, H. (1992) Molecular structure of the arthropod hemocyanins, Adv. Comp. Environ. Physiol. 13, 325-376.
    • (1992) Adv. Comp. Environ. Physiol. , vol.13 , pp. 325-376
    • Markl, J.1    Decker, H.2
  • 41
    • 0026022362 scopus 로고
    • Specific IgG activity of sera from Egyptian schistosomiasis patients to keyhole limpet hemocyanin (KLH)
    • Markl, J., Nour el Din, M., Winter-Siemanowski, S. & Siemanowski, U. A. (1991a) Specific IgG activity of sera from Egyptian schistosomiasis patients to keyhole limpet hemocyanin (KLH), Naturwissenschaften 78, 30-31.
    • (1991) Naturwissenschaften , vol.78 , pp. 30-31
    • Markl, J.1    Nour El Din, M.2    Winter-Siemanowski, S.3    Siemanowski, U.A.4
  • 43
    • 0013569799 scopus 로고
    • The structure of Octopus dofleini hemocyanin
    • Miller, K. I. & van Holde, K. E. (1982) The structure of Octopus dofleini hemocyanin, Comp. Biochem. Physiol. B 73, 1013-1018.
    • (1982) Comp. Biochem. Physiol. B , vol.73 , pp. 1013-1018
    • Miller, K.I.1    Van Holde, K.E.2
  • 44
    • 0025128627 scopus 로고
    • Arrangement of subunits and domains within the Octopus dofleini hemocyanin molecule
    • Miller, K. I., Schabtach, E. & van Holde, K. E. (1990) Arrangement of subunits and domains within the Octopus dofleini hemocyanin molecule, Proc. Natl Acad. Sci. USA 87, 1496-1500.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1496-1500
    • Miller, K.I.1    Schabtach, E.2    Van Holde, K.E.3
  • 45
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • Müller, S. A., Goldie, K. N., Bürki, R., Häring, R. & Engel, A. (1992) Factors influencing the precision of quantitative scanning transmission electron microscopy, Ultramicroscopy 46, 317-334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Bürki, R.3    Häring, R.4    Engel, A.5
  • 46
    • 0022518526 scopus 로고
    • Structure of tabacco mosaic virus at 3.6 Å resolution: Implications for assembly
    • Namba, K. & Stubbs, G. (1986) Structure of tabacco mosaic virus at 3.6 Å resolution: implications for assembly, Science 231, 1401-1406.
    • (1986) Science , vol.231 , pp. 1401-1406
    • Namba, K.1    Stubbs, G.2
  • 48
    • 0031583477 scopus 로고    scopus 로고
    • Structure of keyhole limpet hemocyanin Type 1 (KLH1) at 15 Å resolution by electron microscopy and angular reconstitution
    • in the press
    • Orlova, E. V., Dube, P., Harris, J. R., Beckman, E., Zemlin, F., Markl, J. & van Heel, M. (1997) Structure of keyhole limpet hemocyanin Type 1 (KLH1) at 15 Å resolution by electron microscopy and angular reconstitution, J. Mol. Biol. 272, in the press.
    • (1997) J. Mol. Biol. , vol.272
    • Orlova, E.V.1    Dube, P.2    Harris, J.R.3    Beckman, E.4    Zemlin, F.5    Markl, J.6    Van Heel, M.7
  • 52
    • 0026718875 scopus 로고
    • Immunotherapeutic alternatives in superficial bladder cancer
    • Sargent, E. R. & Williams, R. D. (1992) Immunotherapeutic alternatives in superficial bladder cancer, Urol. Clin. N. Am. 19, 581-589.
    • (1992) Urol. Clin. N. Am. , vol.19 , pp. 581-589
    • Sargent, E.R.1    Williams, R.D.2
  • 53
    • 0002051194 scopus 로고
    • Hemocyanin of the giant keyhole limpet, Megathura crenulata
    • Lamy, J. & Lams, J., eds Dekker, New York
    • Senozan, N. M., Landrum, J., Bonaventura, J. & Bonaventura, C. (1981) Hemocyanin of the giant keyhole limpet, Megathura crenulata. In Invertebrate oxygen binding proteins (Lamy, J. & Lams, J., eds) pp. 703-717, Dekker, New York.
    • (1981) Invertebrate Oxygen Binding Proteins , pp. 703-717
    • Senozan, N.M.1    Landrum, J.2    Bonaventura, J.3    Bonaventura, C.4
  • 54
    • 0016317049 scopus 로고
    • Structure and properties of hemocyanin. XIV. Reassociation of Helix pomatia α-hemocyanin
    • Siezen, R. J. (1974) Structure and properties of hemocyanin. XIV. Reassociation of Helix pomatia α-hemocyanin, J. Mol. Biol. 90, 103-113.
    • (1974) J. Mol. Biol. , vol.90 , pp. 103-113
    • Siezen, R.J.1
  • 55
    • 0016349612 scopus 로고
    • Structure and properties of hemocyanins. XII. Electron microscopy of dissociation products of Helix pomatia α-hemocyanin: Quaternary structure
    • Siezen, R. J. & van Bruggen, E. F. J. (1974) Structure and properties of hemocyanins. XII. Electron microscopy of dissociation products of Helix pomatia α-hemocyanin: quaternary structure, J. Mol. Biol. 90, 77-89.
    • (1974) J. Mol. Biol. , vol.90 , pp. 77-89
    • Siezen, R.J.1    Van Bruggen, E.F.J.2
  • 56
    • 0028227383 scopus 로고
    • Immunotherapy with keyhole limpet hemocyanin: Efficacy and safety in the MB-49 intravesical murine bladder tumor model
    • Swerdlow, R. D., Ratliff, T. L., La Regina, M., Ritchey, J. K. & Ebert, R. F. (1994) Immunotherapy with keyhole limpet hemocyanin: efficacy and safety in the MB-49 intravesical murine bladder tumor model, J. Urol. 151, 1718-1722.
    • (1994) J. Urol. , vol.151 , pp. 1718-1722
    • Swerdlow, R.D.1    Ratliff, T.L.2    La Regina, M.3    Ritchey, J.K.4    Ebert, R.F.5
  • 57
    • 0029916810 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin: Structural and functional characterization of two different subunits and multimers
    • Swerdlow, R. D., Ehert, R. F., Lee, P., Bonaventura, C. & Miller, K. I. (1996) Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers, Comp. Biochem. Physiol. 113B, 537-548.
    • (1996) Comp. Biochem. Physiol. , vol.113 B , pp. 537-548
    • Swerdlow, R.D.1    Ehert, R.F.2    Lee, P.3    Bonaventura, C.4    Miller, K.I.5
  • 59
    • 0018533602 scopus 로고
    • Structure of Helix pomatia oxy-β-hemocyanin and deoxy-β-hemocyanin tubular polymers
    • van Breemen, J. F. L., Ploegman, J. H. & van Bruggen, E. F. J. (1979) Structure of Helix pomatia oxy-β-hemocyanin and deoxy-β-hemocyanin tubular polymers, Eur. J. Biochem. 100, 61-65.
    • (1979) Eur. J. Biochem. , vol.100 , pp. 61-65
    • Van Breemen, J.F.L.1    Ploegman, J.H.2    Van Bruggen, E.F.J.3
  • 62
    • 0026090567 scopus 로고
    • Assembly of Octopus dofleini hemocyanin, A study of the kinetics by sedimentation, light scattering, and electron microscopy
    • van Holde, K. E., Miller, K., Schabtach, E. & Libertini, L. (1991) Assembly of Octopus dofleini hemocyanin, A study of the kinetics by sedimentation, light scattering, and electron microscopy, J. Mol. Biol. 217, 307-321.
    • (1991) J. Mol. Biol. , vol.217 , pp. 307-321
    • Van Holde, K.E.1    Miller, K.2    Schabtach, E.3    Libertini, L.4
  • 63
    • 0022526226 scopus 로고
    • Mass mapping with the scanning transmission electron microscope
    • Wall, J. S. & Hainfeld, J. F. (1986) Mass mapping with the scanning transmission electron microscope, Annu. Rev. Biophys. Biophys. Chem. 15, 355-376.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 355-376
    • Wall, J.S.1    Hainfeld, J.F.2
  • 64
    • 0024280221 scopus 로고
    • Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and polyvinylidene difluoride membrane
    • Walsh, M. J., McDougall, J. & Wittman-Liebold, B. (1988) Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and polyvinylidene difluoride membrane, Biochemistry 27, 6867-6876.
    • (1988) Biochemistry , vol.27 , pp. 6867-6876
    • Walsh, M.J.1    McDougall, J.2    Wittman-Liebold, B.3
  • 65
    • 0015882643 scopus 로고
    • Crossed immunoelectrophoresis
    • Wecke, B. (1973) Crossed immunoelectrophoresis, Scand. J. Immunol. 2 (Suppl. 1), 47-56.
    • (1973) Scand. J. Immunol. , vol.2 , Issue.1 SUPPL. , pp. 47-56
    • Wecke, B.1
  • 67
    • 0029060612 scopus 로고
    • Keyhole limpet hemocyanin contains Gal(β1-3)-GalNAc determinants that are cross-reactive with the T antigen
    • Wirguin, I., Suturkova-Miloscvic, L., Briani, C. & Latov, N. (1995) Keyhole limpet hemocyanin contains Gal(β1-3)-GalNAc determinants that are cross-reactive with the T antigen, Cancer Immunol. Immunother. 40, 307-310.
    • (1995) Cancer Immunol. Immunother. , vol.40 , pp. 307-310
    • Wirguin, I.1    Suturkova-Miloscvic, L.2    Briani, C.3    Latov, N.4
  • 68
    • 0028942120 scopus 로고
    • Keyhole-limpet hemocyanin immunotherapy in the bilharzial bladder: A new treatment modality? Phase II trial: superficial bladder cancer
    • Wishahi, M. M., Ismail, I. M., Ruebben, H. & Otto, T. (1995) Keyhole-limpet hemocyanin immunotherapy in the bilharzial bladder: a new treatment modality? Phase II trial: superficial bladder cancer, J. Urol. 153, 926-928.
    • (1995) J. Urol. , vol.153 , pp. 926-928
    • Wishahi, M.M.1    Ismail, I.M.2    Ruebben, H.3    Otto, T.4


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