L5385
α-Lactalbumin from bovine milk
Type I, ≥85% (PAGE), lyophilized powder
Synonym(s):
Bos d 4, Lactose synthase B protein, alpha-lactalbumin
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About This Item
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biological source
bovine milk
type
Type I
Assay
≥85% (PAGE)
form
lyophilized powder
technique(s)
cell culture | mammalian: suitable
electrophoresis: suitable
solubility
H2O: soluble 10 mg/mL, clear to slightly hazy, colorless to faintly yellow
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... LALBA(281894)
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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 has been used as a supplement of basal medium for various cell cultures. It has also been used as a marker for sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Biochem/physiol Actions
α-Lactalbumin is the cheif protein in human milk. It 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 Α° resolution, demonstrating four α-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. 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.
Quality
Calcium saturated. May have traces of ammonium sulfate and sodium phosphate
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Formation of nanotubes from partially hydrolysed α-lactalbumin (α-La) was investigated at five pH values, two concentrations of α-La and two calcium levels. Nanotubes were formed under almost all combinations of the investigated factors, and for the first time the formation
Daniel Rusu et al.
The Journal of nutrition, 140(2), 382-391 (2009-12-25)
Innate immunity depends on the efficiency of neutrophils to be activated rapidly to restore homeostasis. It can benefit from priming agents that enhance neutrophil capacity to respond more efficiently to a subsequent stimulation. Among natural products, a bovine whey protein
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M J Kronman et al.
The Journal of biological chemistry, 256(16), 8582-8587 (1981-08-25)
Removal of the tightly bound Ca2+ ion from bovine alpha-lactalbumin (Hiraoka et al. (1980) Biochem. Biophys. Res. Commun. 95, 1098-1104) produces a pronounced conformational change, as indicated by fluorescence and absorbance changes. These changes closely resemble the changes that occur
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