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Lactalbumin, alpha-

alpha-Lactalbumin, alpha-lactalbumin, a, LALBA
This gene encodes alpha-lactalbumin, a principal protein of milk. Alpha-lactalbumin forms the regulatory subunit of the lactose synthase (LS) heterodimer and beta 1,4-galactosyltransferase (beta4Gal-T1) forms the catalytic component. Together, these proteins enable LS to produce lactose by transfering galactose moieties to glucose. As a monomer, alpha-lactalbumin strongly binds calcium and zinc ions and may possess bactericidal or antitumor activity. A folding variant of alpha-lactalbumin, called HAMLET, likely induces apoptosis in tumor and immature cells. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, beta-lactoglobulin, Lysozyme
Papers on alpha-Lactalbumin
The effect of long-term under- and overfeeding on the expression of six major milk proteins' genes in the mammary tissue of goats.
Zervas et al., Athens, Greece. In J Anim Physiol Anim Nutr (berl), Dec 2015
In this study, the effect of long-term under- and overfeeding on the expression of as1-casein: CSN1S1, as2-casein: CSN1S2, β-casein: CSN2, κ-casein: CSN3, α-lactalbumin: LALBA and β-lactoglobulin: BLG gene in goat mammary tissue (MT) was examined.
Variability of the caprine whey protein genes and their association with milk yield, composition and renneting properties in the Sarda breed. 1. The LALBA gene.
Vacca et al., Sassari, Italy. In J Dairy Res, Nov 2015
The 5' flanking region and 3' UTR of the caprine LALBA gene were analysed by SSCP and sequencing.
Structure and Potential Cellular Targets of HAMLET-like Anti-Cancer Compounds made from Milk Components.
Church et al., Sydney, Australia. In J Pharm Pharm Sci, Nov 2015
The HAMLET family of compounds (Human Alpha-lactalbumin Made Lethal to Tumours) was discovered during studies on the properties of human milk, and is a class of protein-lipid complexes having broad spectrum anti-cancer, and some specific anti-bacterial properties.
The effect of long term under- and over-feeding on the expression of six major milk protein genes in the mammary tissue of sheep.
Zervas et al., Athens, Greece. In J Dairy Res, Aug 2015
In this study, the effect of long term under- and over-feeding on the expression of αs1-casein: CSN1S1, αs2-casein: CSN1S2, β-casein: CSN2, κ-casein: CSN3, α-lactalbumin: LALBA and β-lactoglobulin: BLG gene in sheep mammary tissue (MT) was examined.
Protein receptor-independent plasma membrane remodeling by HAMLET: a tumoricidal protein-lipid complex.
Svanborg et al., Lund, Sweden. In Sci Rep, 2014
This view emerges from the extraordinary manner in which HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) kills a wide range of tumor cells in vitro and demonstrates therapeutic efficacy and selectivity in cancer models and clinical studies.
Effects of macromolecular crowding on the structural stability of human α-lactalbumin.
Liang et al., Wuhan, China. In Acta Biochim Biophys Sin (shanghai), 2012
analysis of macromolecular crowding on the structural stability of human alpha-lactalbumin
Characterization of an alternative low energy fold for bovine α-lactalbumin formed by disulfide bond shuffling.
Smith et al., Oxford, United Kingdom. In Proteins, 2012
alphaLA forms a misfolded disulfide bond shuffled isomer, X-alphaLA which represents a different low energy fold for the protein; binding calcium plays an important role in both maintaining the native structure of alphaLA and providing a mechanism for distinguishing between folded and misfolded species.
[Alpha-Lactalbumin as an ingredient of infant formula].
Martínez Graciá et al., Murcia, Spain. In Arch Latinoam Nutr, 2012
Alpha-Lactalbumin is the main whey protein in human milk rising 2,44 g/L in mature milk.
Alpha-lactalbumin in human milk alters the proteolytic degradation of soluble CD14 by forming a complex.
Altosaar et al., Ottawa, Canada. In Pediatr Res, 2010
Data show that alpha-lactalbumin and CD14 form a complex in the gut which alters degradation of CD14, suggesting a mechanism by which this key LPS receptor may remain functional in the neonatal gut.
Organization and dynamics of tryptophans in the molten globule state of bovine alpha-lactalbumin utilizing wavelength-selective fluorescence approach: comparisons with native and denatured states.
Chattopadhyay et al., Hyderābād, India. In Biochem Biophys Res Commun, 2010
the organization and dynamics of the functionally important tryptophan residues of BLA in native, molten globule and denatured states utilizing the wavelength-selective fluorescence approach were explored.
The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.
Carver et al., Cardiff, United Kingdom. In Mol Vis, 2009
Structural features of the alphaB-crystallin oligomer when complexed with target proteins under mild stress conditions, i.e., reduction of alpha-lactalbumin at 37 degrees C and malate dehydrogenase when heated at 42 degrees C, were investigated.
Molecular and biotechnological advances in milk proteins in relation to human health.
Sehgal et al., Geelong, Australia. In Curr Protein Pept Sci, 2009
4) alpha-Lactalbumin [LA] demonstrates antiviral, antitumor and anti-stress properties.
Can misfolded proteins be beneficial? The HAMLET case.
Svanborg et al., Lund, Sweden. In Ann Med, 2008
Here we present HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) as an example where partial unfolding and the incorporation of cofactor create a complex with new, beneficial properties.
[Therapeutic properties of proteins and peptides from colostrum and milk].
Artym et al., Taipei, Taiwan. In Postepy Hig Med Dosw (online), 2004
Alpha-lactalbumin (LA) demonstrated antiviral, antitumoral and anti-stress properties.
Nutritional and physiologic significance of alpha-lactalbumin in infants.
Lien et al., Davis, United States. In Nutr Rev, 2003
alpha-Lactalbumin is the major protein in breast milk (20-25% of total protein) and has been described to have several physiologic functions in the neonatal period.
Alpha-lactalbumin possesses a novel calcium binding loop.
Phillips et al., In Nature, 1986
The high-resolution X-ray structure of alpha-lactalbumin reveals a Ca2+ binding fold that resembles an EF-hand only superficially and presumably has no evolutionary relationship with it.
Similarity of the nucleotide sequences of rat alpha-lactalbumin and chicken lysozyme genes.
Safaya et al., In Nature, 1984
alpha-Lactalbumin (alpha-LA) is a milk protein that interacts with the enzyme galactosyltransferase, modifying its substrate specificity in a way which promotes the transfer of galactose to glucose, resulting in a way which promotes the transfer of galactose to glucose, resulting in a beta-1----4 glycosidic linkage and the synthesis of lactose.
alpha-Lactalbumin is not a marker of human hormone-dependent breast cancer.
Campbell et al., In Nature, 1981
Unfortunately this has not been proved, largely because of inconsistencies in the immunoassay procedures used to identify milk proteins, in particular alpha-lactalbumin, in tissue extracts or serum.
alpha-Lactalbumin-casein induction in virgin mouse mammary explants: dose-dependent differential action of cortisol.
Oka et al., In Science, 1980
The interplay of insulin, cortisol, and prolactin induces synthesis of casein and alpha-lactalbumin in cultured mammary explants from mature virgin mice.
Alpha-lactalbumin production in human mammary carcinoma.
McGrath et al., In Science, 1975
Alpha-Lactalbumin was isolated from mature human milk and utilized as an immunogen in rabbits.
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