ChemicalBook--->CAS DataBase List--->9013-90-5

9013-90-5

9013-90-5 Structure

9013-90-5 Structure
IdentificationBack Directory
[Name]

LACTALBUMIN
[CAS]

9013-90-5
[Synonyms]

EC 2.4.1.22
LACTALBUMIN
Lactalbumins
ALBUMIN LACTIC
ALBUMIN (MILK)
ALPHA-LACTALBUMIN
BOVINEALPHA-LACTALBUMIN
COW'SMILKALPHA-LACTALBUMIN
[EINECS(EC#)]

232-750-1
[Molecular Formula]

n.a.
[MDL Number]

MFCD00130492
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[form ]

lyophilized powder
[biological source]

bovine
[Uses]

Lactalbumin is a milk protein obtained from whey by acidifying to ph 5.2, the isoelectric point, followed by coagulation by heat. it is not coagulated by rennin as is casein and is nonfunctional in its properties. it is used for nutritional purposes as a source of protein. it is used in cereals and breads where its relative inertness minimizes complications caused by other milk proteins during baking. it is also termed milk albuminate.
[CAS DataBase Reference]

9013-90-5
[EPA Substance Registry System]

Lactalbumins (9013-90-5)
Safety DataBack Directory
[Hazard Codes ]

B,T
[Risk Statements ]

23/24/25-36/37/38
[Safety Statements ]

26-36/37/39-45
[WGK Germany ]

3
[F ]

10
Hazard InformationBack Directory
[Definition]

LACTALBUMIN is a protein, belonging to the albumins, derived from milk.
[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.
[Biochem/physiol Actions]

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. 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 kDa), and it has a three-dimensional structure with 1.7 Angstrom resolution, demonstrating four a-helices and a triple stranded antiparallel β-sheet.
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