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L5385

Sigma-Aldrich

α-Lactalbumin from bovine milk

Type I, ≥85% (PAGE), lyophilized powder

Synonyme(s) :

Bos d 4, Lactose synthase B protein, alpha-lactalbumin

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About This Item

Numéro CAS:
9051-29-0
Numéro MDL:
MFCD00162025
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

bovine milk

Niveau de qualité

300

Type

Type I

Pureté

≥85% (PAGE)

Forme

lyophilized powder

Technique(s)

cell culture | mammalian: suitable
electrophoresis: suitable

Solubilité

H2O: soluble 10 mg/mL, clear to slightly hazy, colorless to faintly yellow

Numéro d'accès UniProt

P00711

Température de stockage

−20°C

Informations sur le gène

cow ... LALBA(281894)

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Catégories apparentées

Description générale

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).

Actions biochimiques/physiologiques

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.

Qualité

Calcium saturated. May have traces of ammonium sulfate and sodium phosphate

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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Falk Bernsmann et al.
Journal of colloid and interface science, 344(1), 54-60 (2010-01-23)
We recently showed the possibility to build dopamine-melanin films of controlled thickness by successive immersions of a substrate in alkaline solutions of dopamine [F. Bernsmann, A. Ponche, C. Ringwald, J. Hemmerlé, J. Raya, B. Bechinger, J.-C. Voegel, P. Schaaf, V.
Effect of different exogenous fatty acids on the cytosolic triacylglycerol content in bovine mammary cells
Vargas-Bello-Perez E, et al.
Animal Nutrition, 5(2), 202-208 (2019)
Identification of Mannose-Binding Protein from Milkfish (Chanos chanos F.) Serum
Argayosa AM, et al.
Journal of Mathematics, 6(3) (2019)
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
Brandye M Smith et al.
Analytical chemistry, 74(14), 3386-3391 (2002-07-26)
Principal component regression (PCR) was applied to a spectral library of proteins in H2O solution acquired by single-pass attenuated total reflectance (ATR) Fourier transform infrared (FT-IR) spectroscopy. PCR was used to predict the secondary structure content, principally alpha-helical and the
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