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Ovotransferrin
Crystal Structure of chicken egg Ovotransferrin (Ref. 7)

Ovotransferrin

Item Id: FSB1002
Your Price:
$50.00
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Amount
50 mg [$50]
100 mg [$90]
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Ovotransferrin (or conalbumin) is a 686 amino acid glycoprotein from chicken egg white [1], which is expressed as a 705 amino acid pro-protein with a 19 amino acid glycosylation signal sequence that is ultimately cleaved [2]. Ovotransferrin has a single N-linked glycosylation located in the second domain at N492 [3, 4] that corresponds to a molecular weight of about 77.3 kilodaltons (deglycosylated weight of 75.9 kilodaltons) [5, 6]. The structure of ovotransferrin is made up of two transferrin-like domains that are stabilized by six disulfide bonds in the first domain and nine in the second [7, 8]. Each domain can bind one Fe3+ and one carbonate molecule coordinated by a four amino acid Asp-Tyr-Tyr-His motif and a Tyr-Arg-Ala-Gly motif [7], respectively. Apo-ovotransferrin (0-Fe3+) has two apparent isoelectric points (pI) at 6.09 (minor) and 6.24 (major), whereas mono-ovotransferrin (1-Fe3+) has a pI at 6.68, and holo-ovotransferrin (2-Fe3+) has a pI at 7.17 [9]. Absent bicarbonate, ovotransferrin can form a complex with iron and EDTA (iron-ovotransferrin-EDTA) that has an optical peak that can be observed near 490 nm, and with bicarbonate it can form an iron-ovotransferrin-CO3(-) complex has an optical peak near 470 nm [10]. At pH 7 the apo form has a thermal denaturation near 60C, where as the holo form denatures near 65C [11].



Properties

Quantity100 mg
Purity>95% by SDS-PAGE
Molecular Weight77.3 kDa (glycosylated), 75.9 kDa (deglycosylated)
Extinction coefficient1 mg/ml = 1.16/cm path length (Calculated) at 280 nm
Theoretical pI0-Fe3+: 6.09-6.24, 1-Fe3+: 6.68, 2-Fe3+: 7.17
StorageFormat: Liquid
Buffer: 20 mM Tris - pH 8.0, 80 mM NaCl
Temperature: 4C



References

  1. Williams J, Elleman TC, Kingston IB, Wilkins AG, Kuhn KA (1982) The primary structure of hen ovotransferrin Eur J Biochem 122(2):297-303
  2. Thibodeau SN, Lee DC, Palmiter RD (1978) Identical precursors for serum transferrin and egg white conalbumin J Biol Chem 253(11):3771-4
  3. Jacquinot PM, Léger D, Wieruszeski JM, Coddeville B, Montreuil J, Spik G. (1994) Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes Glycobiology. 4(5):617-24
  4. Dorland L, Haverkamp J, Vliegenthart JF, Spik G, Fournet B, Montreuil J. (1979) Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin Eur J Biochem. 100(2):569-74
  5. Awadé AC, Moreau S, Mollé D, Brulé G, Maubois JL (1994) Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins J Chromatogr A. 19;677(2):279-88
  6. Mizutani K, Okamoto I, Fujita K, Yamamoto K, Hirose M (2004) Structural and functional characterization of ovotransferrin produced by Pichia pastoris Biosci Biotechnol Biochem 68(2):376-83
  7. Kurokawa H, Mikami B, Hirose M (1995) Crystal structure of diferric hen ovotransferrin at 2.4 A resolution J Mol Biol. 24; 254(2): 196-207
  8. Elleman TC, Williams J. (1970) The amino acid sequences of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin Biochem J. 116(3):515-32
  9. Richards MP, Huang TL. (1997) Metalloprotein analysis by capillary isoelectric focusing J Chromatogr B Biomed Sci Appl. 690(1-2):43-54
  10. Rogers TB, Feeney RE, Meares CF (1977) Interaction of Anions with Iron-Transferrin-Chelate Complexes J Biol Chem 252(22): 8106-12
  11. Cunningham, F. E., and H. Lineweaver. (1965) Stabilization of egg white proteins to pasteurization temperatures above 60C Food Technol. 19:136-141.





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