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R5258

Sigma-Aldrich

Riboflavin Binding Protein from chicken egg white

lyophilized powder

Synonym(s):

Binding Protein, Chicken Egg White Protein, Riboflavin Protein

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.26

biological source

chicken egg white

Quality Level

form

lyophilized powder

concentration

≥50% protein (biuret)

UniProt accession no.

storage temp.

−20°C

Gene Information

chicken ... RBP(396449)

General description

Riboflavin Binding Protein (RBP) comprises of 19 cysteines and corresponds to a molecular weight of 30 kDa. Egg white RBP is produced in the oviduct cells. Chicken egg white RBP contains an N-terminal ligand binding domain and a C-terminal phosphorylated motif.
Riboflavin binding protein (RBP) transports riboflavin through the bloodstream of the laying hen into the eggs, where the vitamin is essential for embryonic growth and development. RBP consists of a single polypeptide chain containing 9 disulfide bonds. It is a glycoprotein containing ~14% carbohydrate, with sugar moieties including galactose, mannose and glucosamine, and is phosphorylated.

Application

Riboflavin Binding Protein from chicken egg white may be used in fluorescence quenching experiments.

Biochem/physiol Actions

Riboflavin Binding Protein (RBP) is crucial for normal embryo development. RBP interacts with riboflavin and its analogs. The RBP-riboflavin complex is stabilized by interaction between the isoalloxazyne ring of riboflavin and the tyrosine 75 and tryptophan 156 of residues of RBP. RBP elicits sweet supressing functionality and may interact with the sweet taste receptor.
Riboflavin binding protein binds to flavokinase and regulates its activity.

Preparation Note

Supplied as the riboflavin-depleted apo-form.

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Binding study of riboflavin-binding protein with riboflavin and its analogues by differential scanning calorimetry
Wasylewski M
Journal of Protein Chemistry, 19(6), 523-528 (2000)
Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners
Maehashi K, et al.
Chemical Senses, 32(2), 183-190 (2006)
Crystal structure of chicken riboflavin-binding protein
Monaco HL
The Embo Journal, 16(7), 1475-1483 (1997)
Electrochemistry of riboflavin-binding protein and its interaction with riboflavin
Bartovsik M, et al.
Bioelectrochemistry, 76(1-2), 70-75 (2009)
The effect of riboflavin binding protein (RPB) on flavokinase catalytic activity.
Slomczynska, M.
Comparative Biochemistry and Physiology, 87, 681-685 (1987)

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