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Volumn 73, Issue 7, 2005, Pages 341-349

Developmental expression of two Haliotis asinina hemocyanin isoforms

Author keywords

Development; Expression; Haliotis; Hemocyanin; In situ hybridization

Indexed keywords

HEMOCYANIN; COMPLEMENTARY DNA; ISOPROTEIN;

EID: 33644824973     PISSN: 03014681     EISSN: 14320436     Source Type: Journal    
DOI: 10.1111/j.1432-0436.2005.00035.x     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 0034997129 scopus 로고    scopus 로고
    • Rhogocytes (pore cells) as the site of hemocyanin biosynthesis in the marine gastropod Haliotis tuberculata
    • Albrecht U. Keller H. Gebauer W. Markl J. ( 2001) Rhogocytes (pore cells) as the site of hemocyanin biosynthesis in the marine gastropod Haliotis tuberculata. Cell Tissue Res 304 : 455 462.
    • (2001) Cell Tissue Res , vol.304 , pp. 455-462
    • Albrecht, U.1    Keller, H.2    Gebauer, W.3    Markl, J.4
  • 2
    • 0036329690 scopus 로고    scopus 로고
    • The archaeogastropod mollusc Haliotis iris: Tissue and blood metabolites and allosteric regulation of haemocyanin function
    • Behrens J.W. Elias J.P. Taylor H.H. Weber R.E. ( 2002) The archaeogastropod mollusc Haliotis iris: tissue and blood metabolites and allosteric regulation of haemocyanin function. J Exp Biol 205 : 253 263.
    • (2002) J Exp Biol , vol.205 , pp. 253-263
    • Behrens, J.W.1    Elias, J.P.2    Taylor, H.H.3    Weber, R.E.4
  • 4
    • 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
  • 5
    • 0033563284 scopus 로고    scopus 로고
    • Controlled cleavage of KLH1 and KLH2 by the V8 protease from Staphylococcus aureus reassociation, electrophoretic and transmission electron microscopy study of peptide fragments
    • Gebauer W. Harris J.R. ( 1999) Controlled cleavage of KLH1 and KLH2 by the V8 protease from Staphylococcus aureus reassociation, electrophoretic and transmission electron microscopy study of peptide fragments. Eur J Biochem 262 : 166 175.
    • (1999) Eur J Biochem , vol.262 , pp. 166-175
    • Gebauer, W.1    Harris, J.R.2
  • 7
    • 0024942004 scopus 로고
    • Scanning transmission electron microscopic study of molluscan hemocyanins in various aggregation states: Comparison with light scattering molecular weights
    • Hamilton M.G. Herskovits T.T. Furcinitti P.S. Wall J.S. ( 1989) Scanning transmission electron microscopic study of molluscan hemocyanins in various aggregation states: comparison with light scattering molecular weights. 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
  • 8
    • 0001439498 scopus 로고
    • Negative staining
    • In: Harris, J.R. (ed.). IRL Press, Oxford, UK
    • Harris J.R. Horne R.W. ( 1991) Negative staining. In : Harris J.R. (ed.). Electron microscopy in biology. IRL Press, Oxford, UK, 203 228.
    • (1991) Electron Microscopy in Biology. , pp. 203-228
    • Harris, J.R.1    Horne, R.W.2
  • 9
    • 0033485264 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH): A biomedical review
    • Harris J.R. Markl J. ( 1999) Keyhole limpet hemocyanin (KLH): a biomedical review. Micron 30 : 597 623.
    • (1999) Micron , vol.30 , pp. 597-623
    • Harris, J.R.1    Markl, J.2
  • 10
    • 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. Markl J. ( 2000) Haliotis tuberculata hemocyanin (HtH): analysis of oligomeric stability of HtH1 and HtH2, and comparison with keyhole limpet hemocyanin KLH1 and KLH2. Micron 31 : 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
  • 11
    • 0024248001 scopus 로고
    • Recent aspects of the subunit organization and dissociation of hemocyanins
    • Herskovits T.T. ( 1988) Recent aspects of the subunit organization and dissociation of hemocyanins. Comp Biochem Physiol 91 : 597 611.
    • (1988) Comp Biochem Physiol , vol.91 , pp. 597-611
    • Herskovits, T.T.1
  • 13
    • 0036935285 scopus 로고    scopus 로고
    • Mox homeobox expression in muscle lineage of the gastropod Haliotis asinina: Evidence for a conserved role in bilaterian myogenesis
    • Hinman V.F. Degnan B.M. ( 2000) Mox homeobox expression in muscle lineage of the gastropod Haliotis asinina: evidence for a conserved role in bilaterian myogenesis. Dev Genes Evol 212 : 141 144.
    • (2000) Dev Genes Evol , vol.212 , pp. 141-144
    • Hinman, V.F.1    Degnan, B.M.2
  • 14
    • 0141453459 scopus 로고    scopus 로고
    • Expression of anterior Hox genes during larval development of the gastropod Haliotis a sinina
    • Hinman V.F. O'Brien E.K. Richards G.S. Degnan B.M. ( 2003) Expression of anterior Hox genes during larval development of the gastropod Haliotis a sinina. Evol Dev 5 : 508 521.
    • (2003) Evol Dev , vol.5 , pp. 508-521
    • Hinman, V.F.1    O'Brien, E.K.2    Richards, G.S.3    Degnan, B.M.4
  • 15
    • 0002237226 scopus 로고    scopus 로고
    • Abalone (Haliotis tuberculata) hemocyanin type 1 (HtH1). Organization of the approximately 400 kDa subunit, and amino acid sequence of its functional units f, g and h
    • Keller H. Lieb B. Altenhein B. Gebauer D. Richter S. Stricker S. Markl J. ( 1999) Abalone (Haliotis tuberculata) hemocyanin type 1 (HtH1). Organization of the approximately 400 kDa subunit, and amino acid sequence of its functional units f, g and h. Eur J Biochem 264 : 27 38.
    • (1999) Eur J Biochem , vol.264 , pp. 27-38
    • Keller, H.1    Lieb, B.2    Altenhein, B.3    Gebauer, D.4    Richter, S.5    Stricker, S.6    Markl, J.7
  • 16
    • 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 , pp. 79-81
    • Kroll, J.1
  • 17
    • 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
  • 18
    • 0028088636 scopus 로고
    • Three-dimensional reconstruction from a frozen-hydrated specimen of the chiton Lepidochiton sp. hemocyanin
    • Lambert O. Boisset N. Taveau J.C. Lamy J.N. ( 1994) Three-dimensional reconstruction from a frozen-hydrated specimen of the chiton Lepidochiton sp. hemocyanin. J Mol Biol 244 : 640 647.
    • (1994) J Mol Biol , vol.244 , pp. 640-647
    • Lambert, O.1    Boisset, N.2    Taveau, J.C.3    Lamy, J.N.4
  • 19
    • 0029073214 scopus 로고
    • Three-dimensional reconstruction of the hemocyanin of the protobranch bivalve mollusc Nucula hanleyi from frozen-hydrated specimens
    • Lambert O. Taveau J.C. Boisset N. Lamy J.N. ( 1995) Three-dimensional reconstruction of the hemocyanin of the protobranch bivalve mollusc Nucula hanleyi from frozen-hydrated specimens. Arch Biochem Biophys 319 : 231 243.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 231-243
    • Lambert, O.1    Taveau, J.C.2    Boisset, N.3    Lamy, J.N.4
  • 20
    • 0032509091 scopus 로고    scopus 로고
    • Intramolecular localization of the functional units of Sepia officinalis hemocyanin by immunoelectron microscopy
    • Lamy J. You V. Taveau J.C. Boisset N. Lamy J.N. ( 1998) Intramolecular localization of the functional units of Sepia officinalis hemocyanin by immunoelectron microscopy. J Mol Biol 284 : 1051 1074.
    • (1998) J Mol Biol , vol.284 , pp. 1051-1074
    • Lamy, J.1    You, V.2    Taveau, J.C.3    Boisset, N.4    Lamy, J.N.5
  • 21
    • 0024293261 scopus 로고
    • CDNA cloning of the Octopus dofleini hemocyanin: Sequence of the carboxyl-terminal domain
    • Lang W.H. ( 1988) cDNA cloning of the Octopus dofleini hemocyanin: sequence of the carboxyl-terminal domain. Biochemistry 27 : 7276 7282.
    • (1988) Biochemistry , vol.27 , pp. 7276-7282
    • Lang, W.H.1
  • 22
    • 0000507850 scopus 로고    scopus 로고
    • Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and h
    • Lieb B. Altenhein B. Lehnert R. Gebauer W. Markl J. ( 1999) Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and h. Eur J Biochem 265 : 134 144.
    • (1999) Eur J Biochem , vol.265 , pp. 134-144
    • Lieb, B.1    Altenhein, B.2    Lehnert, R.3    Gebauer, W.4    Markl, J.5
  • 23
    • 0034007385 scopus 로고    scopus 로고
    • The sequence of a gastropod hemocyanin (HtH1 from Haliotis tuberculata)
    • Lieb B. Altenhein B. Markl J. ( 2000) The sequence of a gastropod hemocyanin (HtH1 from Haliotis tuberculata). J Biol Chem 275 : 5675 5681.
    • (2000) J Biol Chem , vol.275 , pp. 5675-5681
    • Lieb, B.1    Altenhein, B.2    Markl, J.3
  • 25
    • 4644316521 scopus 로고    scopus 로고
    • CDNA sequence, protein structure, and evolution of the single hemocyanin from Aplysia californica, an opisthobranch gastropod
    • Lieb B. Boisguérin V. Gebauer W. Markl J. ( 2004) cDNA sequence, protein structure, and evolution of the single hemocyanin from Aplysia californica, an opisthobranch gastropod. J Mol Evol 59 : 536 545.
    • (2004) J Mol Evol , vol.59 , pp. 536-545
    • Lieb, B.1    Boisguérin, V.2    Gebauer, W.3    Markl, J.4
  • 26
    • 1242322574 scopus 로고    scopus 로고
    • Evolution of molluscan hemocyanins as deduced from DNA sequencing
    • Lieb B. Markl J. ( 2004) Evolution of molluscan hemocyanins as deduced from DNA sequencing. Micron 35 : 117 119.
    • (2004) Micron , vol.35 , pp. 117-119
    • Lieb, B.1    Markl, J.2
  • 28
    • 33745271216 scopus 로고    scopus 로고
    • Did the 8 MDa molluscan hemocyanin didecamer evolve from a 500 kDa ring?
    • p 62 (Proceedings of the 94th Annual Meeting Osnabrück, Germany).
    • Markl J. Meissner U. Lieb B. ( 2001) Did the 8 MDa molluscan hemocyanin didecamer evolve from a 500 kDa ring? Zoology 104, Suppl. IV p 62 (Proceedings of the 94th Annual Meeting Osnabrück, Germany).
    • (2001) Zoology , Issue.1044
    • Markl, J.1    Meissner, U.2    Lieb, B.3
  • 30
    • 0034696758 scopus 로고    scopus 로고
    • Structure of a molluscan hemocyanin didecamer (HtH1 from Haliotis tuberculata) at 12 angstrom resolution by cryoelectron microscopy
    • Meissner U. Dube P. Harris J.R. Stark H. Markl J. ( 2000) Structure of a molluscan hemocyanin didecamer (HtH1 from Haliotis tuberculata) at 12 angstrom resolution by cryoelectron microscopy. J Mol Biol 298 : 21 34.
    • (2000) J Mol Biol , vol.298 , pp. 21-34
    • Meissner, U.1    Dube, P.2    Harris, J.R.3    Stark, H.4    Markl, J.5
  • 31
    • 0032730273 scopus 로고    scopus 로고
    • Structural comparison of cephalopod hemocyanins: Phylogenetic significance
    • Mouche F. Boisset N. Lamy J. Zal F. Lamy J.N. ( 1999) Structural comparison of cephalopod hemocyanins: phylogenetic significance. J Struct Biol 127 : 199 212.
    • (1999) J Struct Biol , vol.127 , pp. 199-212
    • Mouche, F.1    Boisset, N.2    Lamy, J.3    Zal, F.4    Lamy, J.N.5
  • 32
    • 0019823812 scopus 로고
    • Intracellular polymerized haemocyanin in the branchial gland of a cephalopod
    • Muzii E. ( 1981) Intracellular polymerized haemocyanin in the branchial gland of a cephalopod. Cell Tissue Res 220 : 435 438.
    • (1981) Cell Tissue Res , vol.220 , pp. 435-438
    • Muzii, E.1
  • 33
    • 3242689050 scopus 로고    scopus 로고
    • The effect of captivity and diet on KLH isoform ratios in Megathura crenulata Comp
    • Oakes F.R. McTee S. McMullen J. Culver C.S. Morse D.E. ( 2004) The effect of captivity and diet on KLH isoform ratios in Megathura crenulata Comp. Biochem Physiol Part A 138 : 169 173.
    • (2004) Biochem Physiol Part a , vol.138 , pp. 169-173
    • Oakes, F.R.1    McTee, S.2    McMullen, J.3    Culver, C.S.4    Morse, D.E.5
  • 34
  • 35
    • 0030015403 scopus 로고    scopus 로고
    • Immunocytochemical reaction of a haemocyanin antibody in the midgut gland of Nautilus (Cephalopoda, Tetrabranchiata)
    • Ruth P. Blum W. Bille J. ( 1996) Immunocytochemical reaction of a haemocyanin antibody in the midgut gland of Nautilus (Cephalopoda, Tetrabranchiata). Experientia 52 : 549 553.
    • (1996) Experientia , vol.52 , pp. 549-553
    • Ruth, P.1    Blum, W.2    Bille, J.3
  • 36
    • 0030023265 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate (SDS)-based whole-mount in situ hybridization of Xenopus laevis embryos
    • Shain D.H. Zuber M.X. ( 1996) Sodium dodecyl sulfate (SDS)-based whole-mount in situ hybridization of Xenopus laevis embryos. J Biochem Biophys Methods 31 : 185 188.
    • (1996) J Biochem Biophys Methods , vol.31 , pp. 185-188
    • Shain, D.H.1    Zuber, M.X.2
  • 37
    • 0015848390 scopus 로고
    • Haemocyanin production in pore cells of the freshwater snail Lymnaea stagnalis
    • Sminia T. Boer H. ( 1973) Haemocyanin production in pore cells of the freshwater snail Lymnaea stagnalis. Z Zellforsch Mikrosk Anat 145 : 443 445.
    • (1973) Z Zellforsch Mikrosk Anat , vol.145 , pp. 443-445
    • Sminia, T.1    Boer, H.2
  • 38
    • 0017724250 scopus 로고
    • Haemocyanin synthesis in pore cells of the terrestrial snail Helix aspersa
    • Sminia T. Vlugh-van Dallen J.E. ( 1977) Haemocyanin synthesis in pore cells of the terrestrial snail Helix aspersa. Cell Tissue Res 183 : 299 301.
    • (1977) Cell Tissue Res , vol.183 , pp. 299-301
    • Sminia, T.1    Vlugh-Van Dallen, J.E.2
  • 39
    • 0030886451 scopus 로고    scopus 로고
    • Mass determination, subunit organization and control of oligomerization states of keyhole limpet hemocyanin (KLH)
    • Söhngen S.M. Stahlmann A. Harris J.R. Muller S.A. Engel A. Markl J. ( 1997) Mass determination, subunit organization and control of oligomerization states of keyhole limpet hemocyanin (KLH). Eur J Biochem 248 : 602 614.
    • (1997) Eur J Biochem , vol.248 , pp. 602-614
    • Söhngen, S.M.1    Stahlmann, A.2    Harris, J.R.3    Muller, S.A.4    Engel, A.5    Markl, J.6
  • 41
    • 0034734275 scopus 로고    scopus 로고
    • Allostery in very large molecular assemblies
    • (review).
    • van Holde K.E. Miller K.I. van Olden E. ( 2000) Allostery in very large molecular assemblies. Biophys Chem 86 : 165 172 (review).
    • (2000) Biophys Chem , vol.86 , pp. 165-172
    • Van Holde, K.E.1    Miller, K.I.2    Van Olden, E.3
  • 42
    • 0015882643 scopus 로고
    • Crossed immunoelectrophoresis
    • Weeke B. ( 1973) Crossed immunoelectrophoresis. Scand J Immunol 2 (Suppl 1) : 47 56.
    • (1973) Scand J Immunol , vol.2 , Issue.1 , pp. 47-56
    • Weeke, B.1
  • 43
    • 0035108532 scopus 로고    scopus 로고
    • Temperature effects on hemocyanin oxygen binding in an antarctic cephalopod
    • Zielinski S. Sartoris F.J. Portner H.O. ( 2001) Temperature effects on hemocyanin oxygen binding in an antarctic cephalopod. Biol Bull 200 : 67 76.
    • (2001) Biol Bull , vol.200 , pp. 67-76
    • Zielinski, S.1    Sartoris, F.J.2    Portner, H.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.