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Biological source:
chicken egg white
Assay:
≥95% (agarose gel electrophoresis)
Form:
powder
Technique(s):
gel permeation chromatography (GPC): suitable
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Permítanos ayudarleNombre del producto
Conalbumin from chicken egg white, Iron complex
biological source
chicken egg white
assay
≥95% (agarose gel electrophoresis)
form
powder
technique(s)
gel permeation chromatography (GPC): suitable
UniProt accession no.
storage temp.
−20°C
Quality Level
Gene Information
chicken ... TF(396241)
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Application
Conalbumin (CA) is a monomeric glycoprotein that makes up approximately 13% of the albumin found in egg white. The iron complex of CA is more stable to chemical and physical treatments when compared to the uncomplexed proteins. At near neutral conditions, urea denaturation of CA modifies but does not destroy the iron complex.
General description
Iron-carrying proteins conalbumin and serum transferrin are synthesized with identical 19-amino-acid leader sequences that are removed during protein maturation. The leader sequences are presumably involved in secretion of the proteins by endoplasmic reticulum.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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The resistances of conalbumin and its iron complex to physical and chemical treatments.
P R AZARI et al.
Archives of biochemistry and biophysics, 92, 44-52 (1961-01-01)
The denaturation of proteins. IV. Conalbumin and iron(III)-conalbumin in urea solution.
A N GLAZER et al.
Biochimica et biophysica acta, 71, 109-123 (1963-04-02)
Daisuke Shii et al.
Cornea, 29(2), 197-203 (2009-12-22)
We established a T-helper Type 2 (Th2) clone-induced conjunctival eosinophilia model by injecting D10.G.4.1 (D10) cells, a murine Th2 clone, and conalbumin, its specific antigen, into conjunctiva of AKR/J mice. Using this model, we investigated the effect of a coinjection
Alexandra Acero-Lopez et al.
Food chemistry, 135(4), 2245-2252 (2012-09-18)
High pressure processing of ovotransferrin was carried out to study the structural and physiochemical changes of ovotransferrin under various pressure levels. At pH 8 and pressures higher than 200 MPa, a decrease in total sulfhydryl groups and an increase in
S H Moon et al.
Poultry science, 90(11), 2584-2591 (2011-10-20)
The objective of this study was to determine the effect of nisin and selected meat additives (salt, lactate, lactate-diacetate combination, and polyphosphate) on the antimicrobial activities of ovotransferrin (OTF) against the growth of Listeria monocytogenes. A Bioscreen C turbidometer (Oy
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