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Merck
CN

C0880

Conalbumin from chicken egg white

Iron complex

Synonym(s):

Ovotransferrin

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About This Item

CAS Number:
1391-06-6
UNSPSC Code:
12352202
EC Number:
215-727-0
NACRES:
NA.25
MDL number:
MFCD00130856
Biological source:
chicken egg white
Assay:
≥95% (agarose gel electrophoresis)
Form:
powder
Technique(s):
gel permeation chromatography (GPC): suitable

Key Documents

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biological source

chicken egg white

assay

≥95% (agarose gel electrophoresis)

form

powder

technique(s)

gel permeation chromatography (GPC): suitable

UniProt accession no.

P02789

storage temp.

−20°C

Quality Level

300

Gene Information

chicken ... TF(396241)

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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.

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.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

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

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
SLBF8279V
SLBD5059V
086K7053
042K7059
070H8065

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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)
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)
S N Thibodeau et al.
The Journal of biological chemistry, 253(11), 3771-3774 (1978-06-10)
The NH2-terminal sequences of egg white conalbumin and chicken serum transferrin were examined and found to be identical. Conalbumin, when synthesized in a rabbit reticulocyte cell-free translation system, was found to contain an NH2-terminal extension of 19 amino acid residues.
I C Dunn et al.
Animal genetics, 43(4), 410-418 (2012-04-14)
The size and orientation of calcium carbonate crystals influence the structure and strength of the eggshells of chickens. In this study, estimates of heritability were found to be high (0.6) for crystal size and moderate (0.3) for crystal orientation. There
Kimihiko Mizutani et al.
Biochimica et biophysica acta, 1820(3), 203-211 (2011-08-23)
Transferrins are a group of iron-binding proteins including serum transferrin, lactoferrin and ovotransferrin. The structures of transferrins are discussed. The typical transferrin molecules are folded into two homologous lobes. X-ray crystallography revealed that each lobe is further divided into two
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HPLC Analysis of Protein Standards (1) on BIOshell™ A400 Protein C4

For use as a marker in SDS-PAGE; Albumin from chicken egg white, For use as a marker in SDS-PAGE; L-Lactic Dehydrogenase from rabbit muscle, Type XI, lyophilized powder, 600-1,200 units/mg protein

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