L6385
α-Lactalbumin from bovine milk
For use as a marker in SDS-PAGE
Sinônimo(s):
alpha-lactalbumin
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About This Item
fonte biológica
bovine milk
Nível de qualidade
Formulário
powder
peso molecular
~14.2 kDa
embalagem
vial of 5 mg
concentração
>5 mg per vial protein (biuret)
técnica(s)
electrophoresis: suitable
solubilidade
H2O: soluble 10 mg/mL
nº de adesão UniProt
temperatura de armazenamento
2-8°C
Informações sobre genes
cow ... LALBA(281894)
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Descrição geral
α-Lactalbumin is a small, globular, whey protein that has been found in all milk studied to date. It is a metalloprotein of approximately 14 kDa produced in the mammary glands.
Aplicação
α-Lactalbumin from bovine milk is suitable for use:
- as an electrophoresis marker, with a molar mass of approximately 14,200Da
- in a study to investigate selective binding of proteins on charged surface iron oxide nanoparticles via reverse charge parity model
Ações bioquímicas/fisiológicas
α-Lactalbumin consists of a single polypeptide chain with 8 cysteines which form disulfide bridges. α-Lactalbumin binds several metal ions, including calcium, which is thought to play a role in the regeneration of native α-lactalbumin from the reduced, denatured form. α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. The mature protein consists of 123 amino acid residues (14 kD), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four a-helices and a triple stranded antiparallel β-sheet.
Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase.
Alters the substrate specificity of galactosyltransferase to increase the rate of lactose formation; the complex of galactosyltransferase and α-lactalbumin is called lactose synthase. Site-directed mutagenesis of Asp87 or Asp88 to Ala completely abolishes the strong calcium binding affinity and reduces the stimulation of lactose synthase to <3.5% of the maximal rate.
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