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Volumn 1784, Issue 11, 2008, Pages 1617-1624

Reversibility and "pH-T phase diagrams" of Rapana venosa hemocyanin and its structural subunits

Author keywords

Circular dichroism; Electron microscopy; pH stability; Rapana venosa hemocyanin; Transition curves

Indexed keywords

CALCIUM; CARBOHYDRATE DERIVATIVE; HEMOCYANIN; MAGNESIUM;

EID: 54049151143     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.06.004     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 0002261584 scopus 로고
    • Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods
    • Markl J. Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods. Biol. Bull. (Woods Hole) 171 (1986) 90-115
    • (1986) Biol. Bull. (Woods Hole) , vol.171 , pp. 90-115
    • Markl, J.1
  • 3
    • 33644824973 scopus 로고    scopus 로고
    • Developmental expression of two Haliotis asinina hemocyanin isoforms
    • Streit K., Jackson D., Degnan B.M., and Lieb B. Developmental expression of two Haliotis asinina hemocyanin isoforms. Differentiation 73 (2005) 341-349
    • (2005) Differentiation , vol.73 , pp. 341-349
    • Streit, K.1    Jackson, D.2    Degnan, B.M.3    Lieb, B.4
  • 4
  • 5
    • 0027947875 scopus 로고
    • Quaternary structure, subunits and domain patterns of two discrete forms of keyhole limpet hemocyanin: KLH1 and KLH2
    • Gebauer W., Harris J.R., Heid H., Süling M., Hillenbrand R., Söhngen S., Wegener-Strake A., and Markl J. Quaternary structure, subunits and domain patterns of two discrete forms of keyhole limpet hemocyanin: KLH1 and KLH2. Zoology 98 (1994) 51-68
    • (1994) Zoology , vol.98 , pp. 51-68
    • Gebauer, W.1    Harris, J.R.2    Heid, H.3    Süling, M.4    Hillenbrand, R.5    Söhngen, S.6    Wegener-Strake, A.7    Markl, J.8
  • 6
    • 0034007385 scopus 로고    scopus 로고
    • The sequence of a gastropod hemocyanin (HtH1 from Haliotis tuberculata)
    • Lieb B., Altenhein B., and Mark J. The sequence of a gastropod hemocyanin (HtH1 from Haliotis tuberculata). J. Biol. Chem 275 (2000) 5675-5681
    • (2000) J. Biol. Chem , vol.275 , pp. 5675-5681
    • Lieb, B.1    Altenhein, B.2    Mark, J.3
  • 8
    • 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., and Libertini L. Assembly of Octopus dofleini hemocyanin. A study of the kinetics by sedimentation, light scattering and electron microscopy. J. Mol. Biol 217 (1991) 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
  • 9
    • 0028213894 scopus 로고
    • Intermediate states of assembly in the dissociation of gastropod hemocyanin by hydrostatic pressure
    • Bonafe C.F., Araujo J.R.V., and Silva J.L. Intermediate states of assembly in the dissociation of gastropod hemocyanin by hydrostatic pressure. Biochemistry 33 (1994) 2651-2660
    • (1994) Biochemistry , vol.33 , pp. 2651-2660
    • Bonafe, C.F.1    Araujo, J.R.V.2    Silva, J.L.3
  • 10
    • 0030886451 scopus 로고    scopus 로고
    • Mass determination, subunit organization, and control of oligomerization states of keyhole limpet hemocyanin (KLH)
    • Söhngen S.M., Stahlman A., Harris J.B., Müller S.A., Engel A., and Markl J. Mass determination, subunit organization, and control of oligomerization states of keyhole limpet hemocyanin (KLH). Eur. J. Biochem 248 (1997) 602-614
    • (1997) Eur. J. Biochem , vol.248 , pp. 602-614
    • Söhngen, S.M.1    Stahlman, A.2    Harris, J.B.3    Müller, S.A.4    Engel, A.5    Markl, J.6
  • 12
    • 0029669927 scopus 로고    scopus 로고
    • Rapana thomasiana grosse (gastropoda) haemocyanin: spectroscopic studies of the structure in solution and the conformational stability of the native protein and its structural subunits
    • Dolashka P., Genov N., Parvanova K., Voelter W., Geiger M., and Stoeva S. Rapana thomasiana grosse (gastropoda) haemocyanin: spectroscopic studies of the structure in solution and the conformational stability of the native protein and its structural subunits. Biochem. J. 315 (1996) 139-144
    • (1996) Biochem. J. , vol.315 , pp. 139-144
    • Dolashka, P.1    Genov, N.2    Parvanova, K.3    Voelter, W.4    Geiger, M.5    Stoeva, S.6
  • 14
    • 0033233250 scopus 로고    scopus 로고
    • Spectroscopic properties of Carcinus aestuarii hemocyanin and its structural subunits
    • Dolashka-Angelova P., Hristova R., Stoeva S., and Voelter W. Spectroscopic properties of Carcinus aestuarii hemocyanin and its structural subunits. Spectrochim. Acta Part A 55 (1999) 2927-2934
    • (1999) Spectrochim. Acta Part A , vol.55 , pp. 2927-2934
    • Dolashka-Angelova, P.1    Hristova, R.2    Stoeva, S.3    Voelter, W.4
  • 16
    • 0034257950 scopus 로고    scopus 로고
    • Structural and spectroscopic studies of the native hemocyanin from Maia squinado and its structural subunits
    • Dolashka-Angelova P., Stoeva S., Hristova R., Schuetz J., and Voelter W. Structural and spectroscopic studies of the native hemocyanin from Maia squinado and its structural subunits. Spectrochim. Acta Part A 56 (2000) 1985-1999
    • (2000) Spectrochim. Acta Part A , vol.56 , pp. 1985-1999
    • Dolashka-Angelova, P.1    Stoeva, S.2    Hristova, R.3    Schuetz, J.4    Voelter, W.5
  • 18
    • 0035820352 scopus 로고    scopus 로고
    • Isolation and spectroscopic characterization of the structural subunits of keyhole limpet hemocyanin
    • Schütz J., Dolashka-Angelova P., Abrashev R., Nikolov P., and Voelter W. Isolation and spectroscopic characterization of the structural subunits of keyhole limpet hemocyanin. Biochim. Biophys. Acta 1546 (2001) 325-336
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 325-336
    • Schütz, J.1    Dolashka-Angelova, P.2    Abrashev, R.3    Nikolov, P.4    Voelter, W.5
  • 20
    • 0031424961 scopus 로고    scopus 로고
    • Multidomain structure of the Rapana thomasiana (Gastropod) hemocyanin structural subunit RHSS1
    • Stoeva S., Dolashka P., Pervanova K., Genov N., and Voelter W. Multidomain structure of the Rapana thomasiana (Gastropod) hemocyanin structural subunit RHSS1. Comp. Biochem. Physiol. 118B, 4 (1997) 927-934
    • (1997) Comp. Biochem. Physiol. 118B , vol.4 , pp. 927-934
    • Stoeva, S.1    Dolashka, P.2    Pervanova, K.3    Genov, N.4    Voelter, W.5
  • 21
    • 21244461471 scopus 로고    scopus 로고
    • Conformational states of the Rapana thomasiana hemocyanin and its substructures studied by dynamic light scattering and time-resolved fluorescence spectroscopy
    • Georgieva D., Schwark D., Nikolov P., Idakieva K., Parvanova K., Dierks K., Genov N., and Betzel C. Conformational states of the Rapana thomasiana hemocyanin and its substructures studied by dynamic light scattering and time-resolved fluorescence spectroscopy. Biophys J 88 (2005) 1276-1282
    • (2005) Biophys J , vol.88 , pp. 1276-1282
    • Georgieva, D.1    Schwark, D.2    Nikolov, P.3    Idakieva, K.4    Parvanova, K.5    Dierks, K.6    Genov, N.7    Betzel, C.8
  • 22
    • 14744284608 scopus 로고    scopus 로고
    • Different scanning calorimetry of irreversible denaturation of Rapana thomasiana (marine snail, Gastropod) hemocyanin
    • Idakieva K., Parvanova K., and Todinova S. Different scanning calorimetry of irreversible denaturation of Rapana thomasiana (marine snail, Gastropod) hemocyanin. Bioch. Biophys. Acta 1748 (2005) 50-56
    • (2005) Bioch. Biophys. Acta , vol.1748 , pp. 50-56
    • Idakieva, K.1    Parvanova, K.2    Todinova, S.3
  • 24
    • 0034671529 scopus 로고    scopus 로고
    • Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. Structure and intramolecular evolution of the subunits
    • Voit R., Feldmaier-Fuchs G., Schweikardt T., Decker H., and Burmester T. Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. Structure and intramolecular evolution of the subunits. J. Biol. Chem. 15 275 50 (2000) 39339-39344
    • (2000) J. Biol. Chem. 15 , vol.275 , Issue.50 , pp. 39339-39344
    • Voit, R.1    Feldmaier-Fuchs, G.2    Schweikardt, T.3    Decker, H.4    Burmester, T.5
  • 25
    • 0029917969 scopus 로고    scopus 로고
    • The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding
    • Liu Y., and Sturtevant J.M. The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding. Biochemistry 35 (1996) 3059-3062
    • (1996) Biochemistry , vol.35 , pp. 3059-3062
    • Liu, Y.1    Sturtevant, J.M.2
  • 26
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transitions of globular proteins. calorimetric study of chymotrypsinogen, ribonuclease and myoglobin
    • Privalov P.L., Khechinashvili N.N., and Atanasov B.P. Thermodynamic analysis of thermal transitions of globular proteins. calorimetric study of chymotrypsinogen, ribonuclease and myoglobin. Biopolymers 10 (1971) 1865-1890
    • (1971) Biopolymers , vol.10 , pp. 1865-1890
    • Privalov, P.L.1    Khechinashvili, N.N.2    Atanasov, B.P.3
  • 27
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov P.L., and Gill S.J. Stability of protein structure and hydrophobic interaction. Adv. Protein Chem 39 (1988) 191-234
    • (1988) Adv. Protein Chem , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 29
    • 0034121067 scopus 로고    scopus 로고
    • Haliotis tuberculata hemocyanin (HtH): analysis of oligomeric stability of HtH1 and HtH2, and comparison with keyhole limpet hemocyanin KLH1 and KLH2
    • Harris J.R., Scheffler D., Gebauer W., Lehnert R., and Markl J. Haliotis tuberculata hemocyanin (HtH): analysis of oligomeric stability of HtH1 and HtH2, and comparison with keyhole limpet hemocyanin KLH1 and KLH2. Micron 31 (2000) 613-622
    • (2000) Micron , vol.31 , pp. 613-622
    • Harris, J.R.1    Scheffler, D.2    Gebauer, W.3    Lehnert, R.4    Markl, J.5
  • 31
    • 0033485264 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH): a biomedical review
    • Harris J.R., and Markl J. Keyhole limpet hemocyanin (KLH): a biomedical review. Micron 30 (1999) 597-623
    • (1999) Micron , vol.30 , pp. 597-623
    • Harris, J.R.1    Markl, J.2
  • 33
    • 0014220273 scopus 로고
    • Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH and composition; II. Thermodynamic analysis
    • Hermans J., and Acampora G. Reversible denaturation of sperm whale myoglobin. I. Dependence on temperature, pH and composition; II. Thermodynamic analysis. J. Amer. Chem. Soc 89 (1967) 1543-1552
    • (1967) J. Amer. Chem. Soc , vol.89 , pp. 1543-1552
    • Hermans, J.1    Acampora, G.2
  • 34
    • 0014964816 scopus 로고
    • On the reversibility of thermal denaturation of Delphinus delphis ferri myoglobin derivatives
    • Atanasov B.P., and Mitova S. On the reversibility of thermal denaturation of Delphinus delphis ferri myoglobin derivatives. Biophim. Biophys. Acta 214 (1970) 69-82
    • (1970) Biophim. Biophys. Acta , vol.214 , pp. 69-82
    • Atanasov, B.P.1    Mitova, S.2


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