메뉴 건너뛰기




Volumn 46, Issue 11, 2011, Pages 2144-2151

Further characterization of the subunits of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) by SDS-PAGE electrophoresis and MALDI-TOF-MS

Author keywords

Electrophoresis; Extracellular hemoglobin; Glossosocolex paulistus; MALDI TOF MS; Subunits characterization; Subunits molecular masses

Indexed keywords

EXTRACELLULAR; GLOSSOSOCOLEX PAULISTUS; MALDI TOF MS; SUBUNITS CHARACTERIZATION; SUBUNITS MOLECULAR MASSES;

EID: 80053956145     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.08.013     Document Type: Article
Times cited : (25)

References (24)
  • 1
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • R.E. Weber, and S.N. Vinogradov Nonvertebrate hemoglobins: functions and molecular adaptations Physiol Rev 81 2001 570 611
    • (2001) Physiol Rev , vol.81 , pp. 570-611
    • Weber, R.E.1    Vinogradov, S.N.2
  • 3
    • 1242277843 scopus 로고    scopus 로고
    • The stoichiometry of the four linker subunits of Lumbricus terrestris hemoglobin suggests an asymmetric distribution
    • DOI 10.1016/j.micron.2003.10.041
    • S.N. Vinogradov The stoichiometry of the four linker subunits of Lumbricus terrestris hemoglobin suggests an asymmetric distribution Micron 35 2004 127 129 (Pubitemid 38214842)
    • (2004) Micron , vol.35 , Issue.1-2 , pp. 127-129
    • Vinogradov, S.N.1
  • 5
    • 0029862811 scopus 로고    scopus 로고
    • Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris. Roles of subunit equilibria, non-globin linker chains, and valence of the heme iron
    • DOI 10.1074/jbc.271.47.30007
    • H. Zhu, D.W. Ownby, C.K. Riggs, N.J. Nolasco, J.K. Stoops, and A.F. Riggs Assembly of the gigantic hemoglobin of the earthworm Lumbricus terrestris - roles of subunit equilibria, non-globin linker chains, and valence of the heme iron J Biol Chem 271 1996 30007 30021 (Pubitemid 26389639)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.47 , pp. 30007-30021
    • Zhu, H.1    Ownby, D.W.2    Riggs, C.K.3    Nolasco, N.J.4    Stoops, J.K.5    Riggs, A.F.6
  • 6
    • 0025851333 scopus 로고
    • The extracellular hemoglobin of the earthworm, Lumbricus terrestris: Oxygenation properties of isolated chains, trimer, and a reassociated product
    • K. Fushitani, and A.F. Riggs The extracellular hemoglobin of the earthworm, Lumbricus terrestris - oxygenation properties of isolated chains, trimer, and a reassociated product J Biol Chem 266 1991 10275 10281 (Pubitemid 21906799)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.16 , pp. 10275-10281
    • Fushitani, K.1    Riggs, A.F.2
  • 7
    • 67649981402 scopus 로고    scopus 로고
    • High-level production of recombinant Arenicola marina globin chains in Escherichia coli: A new generation of blood substitute
    • T. Harnois, M. Rousselot, H. Rogniaux, and F. Zal High-level production of recombinant Arenicola marina globin chains in Escherichia coli: a new generation of blood substitute Artif Cell Blood Sub 37 2009 106 116
    • (2009) Artif Cell Blood Sub , vol.37 , pp. 106-116
    • Harnois, T.1    Rousselot, M.2    Rogniaux, H.3    Zal, F.4
  • 9
    • 33847105566 scopus 로고    scopus 로고
    • Partial characterization of giant extracellular hemoglobin of Glossoscolex paulistus: A MALDI-TOF-MS study
    • DOI 10.1016/j.ijbiomac.2006.10.005, PII S0141813006003102
    • M.S. Oliveira, L.M. Moreira, and M. Tabak Partial characterization of giant extracellular hemoglobin of Glossoscolex paulistus: a MALDI-TOF-MS study Int J Biol Macromol 40 2007 429 436 (Pubitemid 46282089)
    • (2007) International Journal of Biological Macromolecules , vol.40 , Issue.5 , pp. 429-436
    • Oliveira, M.S.1    Moreira, L.M.2    Tabak, M.3
  • 10
    • 0033884743 scopus 로고    scopus 로고
    • Polypeptide chain composition diversity of hexagonal-bilayer haemoglobins within a single family of annelids, the alvinellidae
    • DOI 10.1046/j.1432-1327.2000.01594.x
    • F. Zal, B.N. Green, P. Martineau, F.H. Lallier, A. Toulmond, and S.N. Vinogradov Polypeptide chain composition diversity of hexagonal-bilayer hemoglobins within a single family of annelids, the alvinellidae Eur J Biochem 267 2000 5227 5236 (Pubitemid 30641320)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.16 , pp. 5227-5236
    • Zal, F.1    Green, B.N.2    Martineu, P.3    Lallier, F.H.4    Toulmond, A.5    Vinogradov, S.N.6    Childress, J.J.7
  • 11
    • 30744458939 scopus 로고
    • Erythrocruorin of Glossoscolex paulistus (oligochaeta, glossoscolecidae) - Dissociation at alkaline pH and its ligand properties as revealed by chemical, immunochemical and electron-microscopy studies
    • N.C. Meirelles, B. Oliveira, E. de Paula, S. Marangoni, and G.M. Rennebeck Erythrocruorin of Glossoscolex paulistus (oligochaeta, glossoscolecidae) - dissociation at alkaline pH and its ligand properties as revealed by chemical, immunochemical and electron-microscopy studies Comp Biochem Physiol 88A 1987 337 379
    • (1987) Comp Biochem Physiol , vol.88 A , pp. 337-379
    • Meirelles, N.C.1    Oliveira, B.2    De Paula, E.3    Marangoni, S.4    Rennebeck, G.M.5
  • 12
    • 58149394841 scopus 로고    scopus 로고
    • On the molecular mass of the extracellular hemoglobin of Glossoscolex paulistus: Analytical ultracentrifugation reexamination
    • F.A.O. Carvalho, P.S. Santiago, J.C. Borges, and M. Tabak On the molecular mass of the extracellular hemoglobin of Glossoscolex paulistus: analytical ultracentrifugation reexamination Anal Biochem 385 2008 257 263
    • (2008) Anal Biochem , vol.385 , pp. 257-263
    • Carvalho, F.A.O.1    Santiago, P.S.2    Borges, J.C.3    Tabak, M.4
  • 13
    • 44049099950 scopus 로고    scopus 로고
    • Dynamic light scattering and optical absorption spectroscopy study of pH and temperature stabilities of the extracellular hemoglobin of Glossoscolex paulistus
    • P.S. Santiago, F. Moura, L.M. Moreira, M.M. Domingues, N.C. Santos, and M. Tabak Dynamic light scattering and optical absorption spectroscopy study of pH and temperature stabilities of the extracellular hemoglobin of Glossoscolex paulistus Biophys J 94 2008 2228 2240
    • (2008) Biophys J , vol.94 , pp. 2228-2240
    • Santiago, P.S.1    Moura, F.2    Moreira, L.M.3    Domingues, M.M.4    Santos, N.C.5    Tabak, M.6
  • 14
    • 0042622492 scopus 로고    scopus 로고
    • Towards a resolution of the long-standing controversy regarding the molecular mass of extracellular erythrocruorin of the earthworm Lumbricus terrestris
    • E. Daniel, A. Lustig, M.M. David, and Y. Tsfadia Towards a resolution of the long-standing controversy regarding the molecular mass of extracellular erythrocruorin of the earthworm Lumbricus terrestris Biochim Biophys Acta 1649 2003 1 15
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 1-15
    • Daniel, E.1    Lustig, A.2    David, M.M.3    Tsfadia, Y.4
  • 15
    • 0027432969 scopus 로고
    • The extracellular hemoglobin of the earthworm, Lumbricus terrestris. Determination of subunit stoichiometry
    • D.W. Ownby, H. Zhu, K. Schneider, R.C. Beavis, B.T. Chait, and A.F. Riggs The extracellular hemoglobin of the earthworm, Lumbricus-terrestris - determination of subunit stoichiometry J Biol Chem 268 1993 13539 13547 (Pubitemid 23307783)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.18 , pp. 13539-13547
    • Ownby, D.W.1    Zhu, H.2    Schneider, K.3    Beavis, R.C.4    Chait, B.T.5    Riggs, A.F.6
  • 17
    • 33745843278 scopus 로고    scopus 로고
    • Lumbricus Erythrocruorin at 3.5 A Resolution: Architecture of a Megadalton Respiratory Complex
    • DOI 10.1016/j.str.2006.05.011, PII S0969212606002504
    • W.E. Royer, H. Sharma, K. Strand, J.E. Knapp, and B. Bhyravbhatla Lumbricus erythrocruorin at 3.5 angstrom resolution: architecture of a megadalton respiratory complex Structure 14 2006 1167 1177 (Pubitemid 44037420)
    • (2006) Structure , vol.14 , Issue.7 , pp. 1167-1177
    • Royer Jr., W.E.1    Sharma, H.2    Strand, K.3    Knapp, J.E.4    Bhyravbhatla, B.5
  • 19
    • 78650670117 scopus 로고    scopus 로고
    • Crystallization and preliminary structural analysis of the giant haemoglobin from Glossoscolex paulistus at 3.2 angstrom
    • J.F.R. Bachega, L. Bleicher, E.R. Horjales, P.S. Santiago, R.C. Garratt, and M. Tabak Crystallization and preliminary structural analysis of the giant haemoglobin from Glossoscolex paulistus at 3.2 angstrom J Synchrotron Radiat 18 2011 24 28
    • (2011) J Synchrotron Radiat , vol.18 , pp. 24-28
    • Bachega, J.F.R.1    Bleicher, L.2    Horjales, E.R.3    Santiago, P.S.4    Garratt, R.C.5    Tabak, M.6
  • 20
    • 33847138548 scopus 로고    scopus 로고
    • Giant extracellular Glossoscolex paulistus Hemoglobin (HbGp) upon interaction with cethyltrimethylammonium chloride (CTAC) and sodium dodecyl sulphate (SDS) surfactants: Dissociation of oligomeric structure and autoxidation
    • DOI 10.1016/j.bbagen.2006.11.005, PII S0304416506003527
    • P.S. Santiago, L.M. Moreira, E.V. de Almeida, and M. Tabak Giant extracellular Glossoscolex paulistus hemoglobin (HbGp) upon interaction with cethyltrimethylammonium chloride (CTAC) and sodium dodecyl sulphate (SDS) surfactants: dissociation of oligomeric structure and autoxidation Biochim Biophys Acta 1770 2007 506 517 (Pubitemid 46281457)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.4 , pp. 506-517
    • Santiago, P.S.1    Moreira, L.M.2    De Almeida, E.V.3    Tabak, M.4
  • 21
    • 33748071136 scopus 로고    scopus 로고
    • SDS (sodium dodecyl sulfate) effect on the autoxidation of the Glossoscolex paulistus giant extracellular hemoglobin: Kinetic studies at pH 7.0 and 9.0
    • DOI 10.1016/j.colsurfb.2006.07.010, PII S0927776506002244
    • A.L. Poli, L.M. Moreira, M. Tabak, and H. Imasato SDS (sodium dodecyl sulfate) effect on the autoxidation of the Glossoscolex paulistus giant extracellular hemoglobin: kinetic studies at pH 7.0 and 9.0 Colloids Surf B 52 2006 96 104 (Pubitemid 44301877)
    • (2006) Colloids and Surfaces B: Biointerfaces , vol.52 , Issue.1 , pp. 96-104
    • Poli, A.L.1    Moreira, L.M.2    Tabak, M.3    Imasato, H.4
  • 22
    • 0031239592 scopus 로고    scopus 로고
    • Fluorescence studies of extracellular hemoglobin of Glossoscolex paulistus in met form obtained from Sephadex gel filtration
    • DOI 10.1016/S0300-9629(96)00448-3, PII S0300962996004483
    • S.C.M. Agustinho, M.H. Tinto, J.R. Perussi, M. Tabak, and H. Imasato Fluorescence studies of extracellular hemoglobin of Glossoscolex paulistus in met form obtained from sephadex gel filtration Comp Biochem Physiol 118A 1998 171 181 (Pubitemid 27319812)
    • (1997) Comparative Biochemistry and Physiology - A Physiology , vol.118 , Issue.1 , pp. 171-181
    • Agustinho, S.C.M.1    Tinto, M.H.2    Perussi, J.R.3    Tabak, M.4    Imasato, H.5
  • 24
    • 78650239108 scopus 로고    scopus 로고
    • Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: Alkaline oligomeric dissociation
    • F.A.O. Carvalho, P.S. Santiago, J.C. Borges, and M. Tabak Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: alkaline oligomeric dissociation Int J Biol Macromol 48 2011 183 193
    • (2011) Int J Biol Macromol , vol.48 , pp. 183-193
    • Carvalho, F.A.O.1    Santiago, P.S.2    Borges, J.C.3    Tabak, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.