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Volumn 54, Issue 1, 2007, Pages 175-182

Isolation and characterisation of crocodile and python ovotransferrins

Author keywords

Crocodile; Crocodylus niloticus; Crocodylus rhombifer; Iron release; N glycans; Ovotransferrin; Python; Python molarus bivittatus

Indexed keywords

ALLIGATOR; AVES; CROCODYLUS NILOTICUS; CROCODYLUS RHOMBIFER; PYTHON MOLURUS BIVITTATUS; REPTILIA; TESTUDINES; VERTEBRATA;

EID: 33947578107     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2007_3284     Document Type: Article
Times cited : (13)

References (29)
  • 3
    • 0035797875 scopus 로고    scopus 로고
    • Ligand variation in the transferrin family: The crystal structure of H249Q mutant of the human transferrin N-lobe as a model for iron binding in insect transferrins
    • Baker HM, Mason AB, He QY, Baker EN (2001) Ligand variation in the transferrin family: the crystal structure of H249Q mutant of the human transferrin N-lobe as a model for iron binding in insect transferrins. Biochemistry 40: 11670-11675.
    • (2001) Biochemistry , vol.40 , pp. 11670-11675
    • Baker, H.M.1    Mason, A.B.2    He, Q.Y.3    Baker, E.N.4
  • 4
    • 0036188896 scopus 로고    scopus 로고
    • Lactoferrin and transferrin: Functional variations on a common structural framework
    • Baker EN, Baker HM, Kidd RD (2002) Lactoferrin and transferrin: functional variations on a common structural framework. Biochem Cell Biol 80: 27-34.
    • (2002) Biochem Cell Biol , vol.80 , pp. 27-34
    • Baker, E.N.1    Baker, H.M.2    Kidd, R.D.3
  • 5
    • 0037388042 scopus 로고    scopus 로고
    • Dealing with iron: Common structural principles in proteins that transport iron and heme
    • Baker HM, Anderson BF, Baker EN (2003) Dealing with iron: common structural principles in proteins that transport iron and heme. Proc Natl Acad Sci USA 100: 3579-3583.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3579-3583
    • Baker, H.M.1    Anderson, B.F.2    Baker, E.N.3
  • 6
    • 0025924788 scopus 로고    scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • Bali PK, Zak O, Aisen P (2001) A new role for the transferrin receptor in the release of iron from transferrin. Biochemistry 30: 324-328.
    • (2001) Biochemistry , vol.30 , pp. 324-328
    • Bali, P.K.1    Zak, O.2    Aisen, P.3
  • 7
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB (1995) Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal Biochem 230: 229-238.
    • (1995) Anal Biochem , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 8
    • 33745229698 scopus 로고    scopus 로고
    • Isolation, cloning and sequencing of transferrins from red-eared turtle, African ostrich, and turkey
    • Ciuraszkiewicz J, Olczak M, Wa̧torek W (2006) Isolation, cloning and sequencing of transferrins from red-eared turtle, African ostrich, and turkey. Comp Biochem Physiol 144B: 301-310.
    • (2006) Comp Biochem Physiol , vol.144 B , pp. 301-310
    • Ciuraszkiewicz, J.1    Olczak, M.2    Wa̧torek, W.3
  • 9
    • 0027360843 scopus 로고
    • Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin release
    • Dewan JC, Mikami B, Hirose M, Sacchettini JC (1993) Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin release. Biochemistry 32: 11963-11968.
    • (1993) Biochemistry , vol.32 , pp. 11963-11968
    • Dewan, J.C.1    Mikami, B.2    Hirose, M.3    Sacchettini, J.C.4
  • 10
    • 27644551255 scopus 로고    scopus 로고
    • The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrin
    • Gianetti AM, Halbrooks PJ, Mason AB, Vogt TM, Enns CA, Björkman PJ (2005) The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrin. Structure 13: 1613-1623.
    • (2005) Structure , vol.13 , pp. 1613-1623
    • Gianetti, A.M.1    Halbrooks, P.J.2    Mason, A.B.3    Vogt, T.M.4    Enns, C.A.5    Björkman, P.J.6
  • 11
    • 13544254423 scopus 로고    scopus 로고
    • Transferrins: Structure, function and potential therapeutic actions
    • Gomme PT, McCann KB (2005) Transferrins: structure, function and potential therapeutic actions. Drug Discov Today 10: 267-273.
    • (2005) Drug Discov Today , vol.10 , pp. 267-273
    • Gomme, P.T.1    McCann, K.B.2
  • 12
    • 28244493040 scopus 로고    scopus 로고
    • Composition of pH-sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release
    • Halbrooks PJ, Giannetti AM, Klein JS, Björkman PJ, Larouche JR, Smith VC, MacGillivray RTA, Everse SJ, Mason AB (2005) Composition of pH-sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release. Biochemistry 44: 15451-15460.
    • (2005) Biochemistry , vol.44 , pp. 15451-15460
    • Halbrooks, P.J.1    Giannetti, A.M.2    Klein, J.S.3    Björkman, P.J.4    Larouche, J.R.5    Smith, V.C.6    MacGillivray, R.T.A.7    Everse, S.J.8    Mason, A.B.9
  • 13
    • 0033609501 scopus 로고    scopus 로고
    • Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: Iron release trigger and anion-binding site
    • He QY, Mason AB, Tam BM, MacGillivray RTA, Woodworth RC (1999) Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: iron release trigger and anion-binding site. Biochemistry 38: 9704-9711.
    • (1999) Biochemistry , vol.38 , pp. 9704-9711
    • He, Q.Y.1    Mason, A.B.2    Tam, B.M.3    MacGillivray, R.T.A.4    Woodworth, R.C.5
  • 14
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kühn LC (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci USA 93: 8175-8182.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 15
    • 0029845404 scopus 로고    scopus 로고
    • Immunoglobulin separation from egg yolk: A serial filtration system
    • Kim H, Nakai S (1996) Immunoglobulin separation from egg yolk: a serial filtration system. J Food Sci 61: 510-513.
    • (1996) J Food Sci , vol.61 , pp. 510-513
    • Kim, H.1    Nakai, S.2
  • 16
    • 11144261515 scopus 로고    scopus 로고
    • Evolution of duplications in the transferrin family of proteins
    • Lambert LA, Perri H, Meehan TJ (2005a) Evolution of duplications in the transferrin family of proteins. Comp Biochem Physiol 140A: 11-25.
    • (2005) Comp Biochem Physiol , vol.140 A , pp. 11-25
    • Lambert, L.A.1    Perri, H.2    Meehan, T.J.3
  • 17
    • 24344475974 scopus 로고    scopus 로고
    • Evolution of transferrin family: Conservation of residues associated with iron and anion binding
    • Lambert LA, Perri H, Halbrooks PJ, Mason AB (2005b) Evolution of transferrin family: conservation of residues associated with iron and anion binding. Comp Biochem Physiol 142B: 129-141.
    • (2005) Comp Biochem Physiol , vol.142 B , pp. 129-141
    • Lambert, L.A.1    Perri, H.2    Halbrooks, P.J.3    Mason, A.B.4
  • 18
    • 0018826551 scopus 로고
    • The chicken transferrin gene. Restriction endonuclease analysis of gene sequences in liver and oviduct DNA
    • Lee DC, McKnight S, Palmiter RD (1980) The chicken transferrin gene. Restriction endonuclease analysis of gene sequences in liver and oviduct DNA. J Biol Chem 255: 1442-1450.
    • (1980) J Biol Chem , vol.255 , pp. 1442-1450
    • Lee, D.C.1    McKnight, S.2    Palmiter, R.D.3
  • 20
    • 0030719461 scopus 로고    scopus 로고
    • Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
    • Moore SA, Anderson BF, Groom CR, Haridas M, Baker EN (1997) Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution. J Mol Biol 274: 222-236.
    • (1997) J Mol Biol , vol.274 , pp. 222-236
    • Moore, S.A.1    Anderson, B.F.2    Groom, C.R.3    Haridas, M.4    Baker, E.N.5
  • 21
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 23
    • 28344457682 scopus 로고    scopus 로고
    • Lactoferrin: An important host defence against microbial and viral attack
    • Valenti P, Antonini G (2005) Lactoferrin: an important host defence against microbial and viral attack. Cell Mol Life Sci 62: 2576-2587.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2576-2587
    • Valenti, P.1    Antonini, G.2
  • 24
    • 0344508909 scopus 로고
    • Receptor-mediated endocytosis of transferrin and the uptake of Fe in K562 cells: Identification of nonlysosomal acidic compartment
    • van Renswoude J, Bridges KR, Harford JB, Klausner RD (1982) Receptor-mediated endocytosis of transferrin and the uptake of Fe in K562 cells: identification of nonlysosomal acidic compartment. Proc Natl Acad Sci USA 79: 6186-6190.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6186-6190
    • van Renswoude, J.1    Bridges, K.R.2    Harford, J.B.3    Klausner, R.D.4
  • 25
    • 17544364169 scopus 로고    scopus 로고
    • Cooperative interactions between the amino- and carboxy-terminal lobes contribute to the unique iron-binding stability of lactoferrin
    • Ward PP, Zhou X, Conneely OM (1996) Cooperative interactions between the amino- and carboxy-terminal lobes contribute to the unique iron-binding stability of lactoferrin. J Biol Chem 271: 12790-12794.
    • (1996) J Biol Chem , vol.271 , pp. 12790-12794
    • Ward, P.P.1    Zhou, X.2    Conneely, O.M.3
  • 26
    • 0025203833 scopus 로고
    • A comparison of the structure and properties of serum transferrin from 17 animal species
    • Welch S (1990) A comparison of the structure and properties of serum transferrin from 17 animal species. Comp Biochem Physiol 97B: 417-427.
    • (1990) Comp Biochem Physiol , vol.97 B , pp. 417-427
    • Welch, S.1
  • 27
    • 0037062620 scopus 로고    scopus 로고
    • The synergistic anion-binding sites of human transferrin: Chemical and physiological effects of site-directed mutagenesis
    • Zak O, Ikuta K, Aisen P (2002) The synergistic anion-binding sites of human transferrin: chemical and physiological effects of site-directed mutagenesis. Biochemistry 41: 7416-7423.
    • (2002) Biochemistry , vol.41 , pp. 7416-7423
    • Zak, O.1    Ikuta, K.2    Aisen, P.3
  • 28
    • 0142095049 scopus 로고    scopus 로고
    • Iron release from transferrin, its C-lobe and their complexes with transferrin receptor: Presence of N-lobe accelerates release from C-lobe at endosomal pH
    • Zak O, Aisen P (2003) Iron release from transferrin, its C-lobe and their complexes with transferrin receptor: presence of N-lobe accelerates release from C-lobe at endosomal pH. Biochemistry 42: 12330-12334.
    • (2003) Biochemistry , vol.42 , pp. 12330-12334
    • Zak, O.1    Aisen, P.2
  • 29
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • Zor T, Selinger Z (1996) Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal Biochem 236: 302-308.
    • (1996) Anal Biochem , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2


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