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biological source
bovine milk
assay
≥90% (PAGE)
form
powder
mol wt
18,363 Da by calculation
technique(s)
HPLC: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... LGB(280838)
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General description
A member of the lipocalin family, βLg is a small protein of 162 amino acids with a molecular mass of ∼18,400 Da, featuring an eight-stranded β-barrel (strands A-H) succeeded by a three-turn a-helix and a final β-strand (strand I) that forms part of the dimerization interface.
Milk from dairy cows contains the protein β-lactoglobulin (BLG). It naturally occurs in a number of genetic variants, and the most prevalent bovine variants are known as BLG A and BLG B.
Application
β-Lactoglobulin A from bovine milk has been used:
- as a calibrant for the calibration of the TriWave device
- as a standard in the detection and quantification of β-lactoglobulin in bovine milk by reverse-phase high performance liquid chromatography (HPLC)
- in the purification and molecular weight measurement of protease samples
β-Lactoglobulin was used in the identification of the genetic variants of κ-casein in milk by isoelectric focusing electrophoresis.
Biochem/physiol Actions
β-Lactoglobulin (β-lg) possesses heat-set gelation properties. It also exhibits antiviral, anticarcinogenic and hypocholesterolemic effects. β-lg can bind to retinol and long-chain fatty acids. It may participate in the absorption and metabolism of fatty acids.
Storage Class
11 - Combustible Solids
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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Laurette Tavel et al.
Journal of agricultural and food chemistry, 56(21), 10208-10217 (2008-10-22)
Interactions between beta-lactoglobulin (BLG) in its monomeric form and a wide range of aroma compounds were investigated by Fourier transform infrared (FT-IR) and 2D nuclear magnetic resonance (NMR) spectroscopies. A screening of the ligands was carried out by FT-IR through
K M Oliveira et al.
European journal of biochemistry, 268(2), 477-483 (2001-02-13)
The crystal structures of beta-lactoglobulin genetic variants A and B have been determined in the orthorhombic space group C222(1) (lattice Y) by X-ray diffraction at 2.0 A and 1.95 A resolution, respectively. The structural comparison shows that both variants exhibit
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The journal of physical chemistry. B, 112(36), 11422-11434 (2008-08-19)
We use time-dependent fluorescence Stokes shift (TDFSS) information to study the fluctuation rates of the lipocalin, beta-lactoglobulin A in the vicinity of an encapsulated coumarin 153 molecule. The system has three unique dielectric environments in which the fluorophore binds. We
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