L6385

α-Lactalbumin from bovine milk

For use as a marker in SDS-PAGE

• Synonim(y): alpha-lactalbumin
• Numer CAS: 9051-29-0
• UNSPSC Code: 12352202
• NACRES: NA.61
• MDL number: MFCD00162025
• Biological source: bovine milk
• Form: powder
• Technique(s): electrophoresis: suitable
• Concentration: >5 mg per vial protein (biuret)

Właściwości

• biological source: bovine milk
• Quality Segment: 200
• form: powder
• mol wt: ~14.2 kDa
• packaging: vial of 5 mg
• concentration: >5 mg per vial protein (biuret)
• technique(s): electrophoresis: suitable
• solubility: H₂O: soluble 10 mg/mL
• UniProt accession no.: P00711
• storage temp.: 2-8°C
• Gene Information: cow ... LALBA(281894)

Opis

General description

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.

Application

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

α-Lactalbumin was used in the reduction of the antigenicity of whey proteins by lactic acid fermentation.

Biochem/physiol Actions

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.

Ta strona może zawierać tekst przetłumaczony maszynowo.