L6385

α-Lactalbumin aus Kuhmilch

For use as a marker in SDS-PAGE

• Synonym(e): alpha-lactalbumin
• CAS-Nummer: 9051-29-0
• MDL-Nummer: MFCD00162025
• UNSPSC-Code: 12352202
• NACRES: NA.61

Eigenschaften

• Biologische Quelle: bovine milk
• Qualitätsniveau: 200
• Form: powder
• Mol-Gew.: ~14.2 kDa
• Verpackung: vial of 5 mg
• Konzentration: >5 mg per vial protein (biuret)
• Methode(n): electrophoresis: suitable
• Löslichkeit: H₂O: soluble 10 mg/mL
• UniProt-Hinterlegungsnummer: P00711
• Lagertemp.: 2-8°C
• Angaben zum Gen: cow ... LALBA(281894)

Beschreibung

Allgemeine Beschreibung

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.[1]

Anwendung

α-Lactalbumin from bovine milk is suitable for use:

• as an electrophoresis marker, with a molar mass of approximately 14,200Da[2][3][4]
• in a study to investigate selective binding of proteins on charged surface iron oxide nanoparticles via reverse charge parity model[5]

α-Lactalbumin was used in the reduction of the antigenicity of whey proteins by lactic acid fermentation.[6]

Biochem./physiol. Wirkung

Verändert die Substratspezifität von Galactosyltransferase und beschleunigt so die Lactosebildung; der Komplex aus Galactosyltransferase und α-Lactalbumin wird Lactose-Synthase genannt.

Verändert die Substratspezifität von Galactosyltransferase und beschleunigt so die Lactosebildung; der Komplex aus Galactosyltransferase und α-Lactalbumin wird Lactose-Synthase genannt. Ortsgerichtete Mutagenese von Asp⁸⁷ oder Asp⁸⁸ an Ala hebt die starke Calcium-Bindungsaffinität vollständig auf und reduziert die Stimulation von Lactose-Synthase auf <3,5 % der Maximalrate.

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.^[7] α-Lactalbumin also has a distinct zinc binding site that is thought to play a role in the binding of the lactose synthase complex. [8][9] 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.[1]