LACTALBUMIN
LACTALBUMIN structure
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Common Name | LACTALBUMIN | ||
|---|---|---|---|---|
| CAS Number | 9013-90-5 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Lipid binding specificity of bovine α-lactalbumin: a multidimensional approach.
Biochim. Biophys. Acta 1838(8) , 2078-86, (2014) Many soluble proteins are known to interact with membranes in partially disordered states, and the mechanism and relevance of such interactions in cellular processes are beginning to be understood. Bovine α-lactalbumin (BLA) represents an excellent prototype ... |
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Electrodynamic pressure modulation of protein stability in cosolvents.
Biochemistry 52(46) , 8363-73, (2013) Cosolvents affect structural stability of proteins in aqueous solutions. A clear understanding of the mechanism by which cosolvents impact protein stability is critical to understanding protein folding in a biological milieu. In this study, we investigated th... |
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Binding of vitamin A by casein micelles in commercial skim milk.
J. Dairy Sci. 96(2) , 790-8, (2013) Recent studies have shown that reassembled micelles formed by caseinates and purified casein fractions (α(s)- and β-casein) bind to hydrophobic compounds, including curcumin, docosahexaenoic acid, and vitamin D. However, limited research has been done on the ... |
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Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.
Proc. Natl. Acad. Sci. U. S. A. 110(46) , E4289-97, (2013) The complex kinetics of Pi and ADP release by the chaperonin GroEL/GroES is influenced by the presence of unfolded substrate protein (SP). Without SP, the kinetics of Pi release are described by four phases: a "lag," a "burst" of ATP hydrolysis by the nascent... |
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Transient transformation of oligomeric structure of alpha-crystallin during its chaperone action.
Int. J. Biol. Macromol. 55 , 62-8, (2013) New evidence for dynamic behavior and flexible oligomeric structure of the molecular chaperone α-crystallin is presented. Based on the results of laser dynamic light scattering, centrifugal ultrafiltration, size exclusion chromatography, analytical ultracentr... |
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Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: potential for native α-lactalbumin purification.
J. Dairy Res. 80(1) , 14-20, (2013) The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7.0, 7.8 and... |
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Magnetic labeling of proteins for atomic force microscopy.
Dokl. Biochem. Biophys. 448 , 33-5, (2013)
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Protein-fatty acid complexes: biochemistry, biophysics and function.
FEBS J. 280(8) , 1733-49, (2013) Thirteen years ago, α-lactalbumin (α-LA) was first reported to form a complex with oleic acid (OA). This complex, called HAMLET (human α-lactalbumin made lethal to tumour cells), was found to be cytotoxic to cancer cells. In HAMLET, α-LA assumes a partially u... |
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Lipids as tumoricidal components of human α-lactalbumin made lethal to tumor cells (HAMLET): unique and shared effects on signaling and death.
J. Biol. Chem. 288(24) , 17460-71, (2013) Long-chain fatty acids are internalized by receptor-mediated mechanisms or receptor-independent diffusion across cytoplasmic membranes and are utilized as nutrients, building blocks, and signaling intermediates. Here we describe how the association of long-ch... |
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The biological activities of protein/oleic acid complexes reside in the fatty acid
Biochim. Biophys. Acta 1834(6) , 1125-43, (2013) A complex formed by human α-lactalbumin (α-LA) and oleic acid (OA), named HAMLET, has been shown to have an apoptotic activity leading to the selective death of tumor cells. In numerous publications it has been reported that in the complex α-LA is monomeric a... |