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Merck

L4385

α-Lactalbumin from bovine milk

Marker for non-denaturing PAGE

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352202
EC Number:
235-747-3
NACRES:
NA.61
MDL number:
Biological source:
bovine milk
Form:
lyophilized powder
Technique(s):
microbiological culture: suitable
Concentration:
0.9—1.4 mg per vial protein (biuret)
Service technique
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biological source

bovine milk

Quality Segment

form

lyophilized powder

mol wt

~14.2 kDa

concentration

0.9—1.4 mg per vial protein (biuret)

technique(s)

microbiological culture: suitable

UniProt accession no.

storage temp.

−20°C

Gene Information

cow ... LALBA(281894)

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 was used in the isolation and analysis of restriction endonuclease digestive patterns of chromosomal DNA from Mycobacterium paratuberculosis and other Mycobacterium species. It was also used in a study to test if the neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins.

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.
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.

Preparation Note

0.9-1.4 mg/mL after reconstitution with 1 mL of water


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Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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