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Merck

L4385

Sigma-Aldrich

α-Lactalbumin from bovine milk

Marker for non-denaturing PAGE

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About This Item

Número de CAS:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine milk

Quality Level

form

lyophilized powder

mol wt

~14.2 kDa

technique(s)

microbiological culture: suitable

UniProt accession no.

storage temp.

−20°C

Gene Information

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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 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. 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.

Reconstitution

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Michael Helwig et al.
The Journal of biological chemistry, 288(2), 1114-1124 (2012-11-23)
Neurodegenerative diseases such as Alzheimer (AD) and Parkinson (PD) are characterized by abnormal aggregation of misfolded β-sheet-rich proteins, including amyloid-β (Aβ)-derived peptides and tau in AD and α-synuclein in PD. Correct folding and assembly of these proteins are controlled by
Comparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme.
K Brew et al.
The Journal of biological chemistry, 242(16), 3747-3749 (1967-08-25)
Gladys Bichang'a et al.
Journal of chemical ecology, 44(11), 1030-1039 (2018-08-08)
Foraging parasitoids use chemical signals in host recognition and selection processes. Although, the volatiles play a relevant role in the localization by parasitoids of their hosts feeding on plants, the host identification process for acceptance occurs mainly during contact between
J Ren et al.
The Journal of biological chemistry, 268(26), 19292-19298 (1993-09-15)
It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A
Why people become psychiatric nurses.
P Jackson
Nursing, 4(10), 32-34 (1990-05-10)

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