Alpha-lactalbumin is a tryptophan-rich protein fraction. A diet enriched with alpha-lactalbumin increases the ratio of tryptophan to the other large neutral amino acids, which may in turn increase brain serotonin content. In stress-vulnerable individuals, alpha-lactalbumin improved mood and attenuated the cortisol response after experimental stress. The aim of the present study was to investiga...

This study describes an alpha-lactalbumin folding variant from human milk with bactericidal activity against antibiotic-resistant and -susceptible strains of Streptococcus pneumoniae. The active complex precipitated with the casein fraction at pH 4.6 and was purified from casein by a combination of anion exchange and gel chromatography. Unlike other casein components, the active complex was ret...

The thermal denaturation of alpha-lactalbumin was studied at pH 7.0 and 9.0 in aqueous 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) by high-sensitivity differential scanning calorimetry. The conformation of the protein was analyzed by a combination of fluorescence and circular dichroism measurements. The most obvious effect of HFIP was lowering of the transition temperature with an increase in the ...

The simultaneous separation of bovine whey proteins [alpha-lactalbumin and beta-lactoglobulin (A+B)] and soybean proteins was performed, for the first time, by capillary electrophoresis. Different experimental conditions were tested. The most suitable consisted of 0.050 M phosphate buffer (pH 8) with 1 M urea and 1.2 mg/ml methylhydroxyethylcellulose, UV detection at 280 nm, 15 kV applied volta...

Removal of the tightly bound Ca2+ ion from bovine a-lactalbumin (Hiraoka et al. (1980) Biochem. Biophys. Res. Commun. 95, 1098-1104) produces a pronounced conformational change, as indicated by fluorescence and absorbance changes. These changes closely resemble the changes that occur on acid denaturation of the native protein. The binding of ions to apo-a-lactalbumin at pH 7.4 has been examined...

An intestinal perfusion technique has been used in normal human subjects to investigate the influence that starter protein composition and hydrolysis procedure have on absorption of amino acid residues from partial enzymic hydrolysates of whole protein. Five starter proteins were studied. Three (egg albumin, casein/soy/lactalbumin, and lactalbumin) were hydrolysed by papain, a second lactalbumi...

Background: Advances in dairy technology make it possible to enrich infant formula with specific bovine milk components that may enhance nutrient status. Glycomacropeptide, a carbohydrate-rich casein peptide, may increase absorption of calcium, iron, or zinc. -Lactalbumin, a major breast-milk protein, may contribute to a balanced amino acid pattern and increase calcium and zinc absorption. Obje...

Serum levels of a-lactalbumin were assayed using a monoclonal antibody specific for this breast specific molecule. Elevated levels were found in 87% (48/55) of sera from women in the third trimester of pregnancy (29.1 ± 7.4 ng ml-'), from 64% (62/97) of patients with breast cancer (23.4 ± 5.6 ng ml-'), and from 70% (56/80) of patients with gynaecological cancers (19.4 ± 6.7 ng ml-'). These x-la...

An intestinal perfusion technique has been used in normal human subjects to investigate the influence that starter protein composition and hydrolysis procedure have on absorption of amino acid residues from partial enzymic hydrolysates of whole protein. Five starter proteins were studied. Three (egg albumin, casein/soy/lactalbumin, and lactalbumin) were hydrolysed by papain, a second lactalbumi...

The complete amino acid sequence of bovine oc-lactalbumin has been established. The unique seq,uence was deduced by characterization of the tryptic, chymotryptic, and peptic peptides isolated from enzymic hydrolysates of the two unique fragments obtained on cleavage of S-aminoethyl-a-lactalbumin with cyanogen bromide as described earlier. Important overlapping peptides were also obtained by seq...