PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16774908-9 2006 The results indicated the presence of N-acetyllactosamine/lactose-binding activity in BLG and provided an effective purification method utilizing the novel carbohydrate binding activity. Lactose 58-65 beta-lactoglobulin Bos taurus 86-89 11829650-0 2002 Maillard reaction induced lactose attachment to bovine beta-lactoglobulin: electrospray ionization and matrix-assisted laser desorption/ionization examination. Lactose 26-33 beta-lactoglobulin Bos taurus 55-73 11829650-1 2002 Nonenzymatic attachment of lactose to beta-lactoglobulin (beta-Lg) was investigated under different conditions. Lactose 27-34 beta-lactoglobulin Bos taurus 38-56 11829650-1 2002 Nonenzymatic attachment of lactose to beta-lactoglobulin (beta-Lg) was investigated under different conditions. Lactose 27-34 beta-lactoglobulin Bos taurus 58-65 10552848-1 1999 Bovine beta-LG was modified by glycation with lactose in a powdered state or in an aqueous solution. Lactose 46-53 beta-lactoglobulin Bos taurus 7-14 2350400-0 1990 In vitro transport of beta-lactoglobulin across the jejunum of lactose-fed rats. Lactose 63-70 beta-lactoglobulin Bos taurus 22-40 10563854-1 1999 The effect of glycation with lactose on the association behavior and conformational state of bovine beta-lactoglobulin (beta-LG) was studied, using size exclusion chromatography, polyacrylamide gel electrophoresis, proteolytic susceptibility, and binding of a fluorescent probe. Lactose 29-36 beta-lactoglobulin Bos taurus 100-118 10563854-1 1999 The effect of glycation with lactose on the association behavior and conformational state of bovine beta-lactoglobulin (beta-LG) was studied, using size exclusion chromatography, polyacrylamide gel electrophoresis, proteolytic susceptibility, and binding of a fluorescent probe. Lactose 29-36 beta-lactoglobulin Bos taurus 120-127 9240451-1 1997 Lactose reacts nonenzymatically with beta-lactoglobulin (beta-LG), the major whey protein, under mild heat treatment and the formation of the complex may be monitored by mass spectrometry. Lactose 0-7 beta-lactoglobulin Bos taurus 37-55 9240451-1 1997 Lactose reacts nonenzymatically with beta-lactoglobulin (beta-LG), the major whey protein, under mild heat treatment and the formation of the complex may be monitored by mass spectrometry. Lactose 0-7 beta-lactoglobulin Bos taurus 57-64 9240451-3 1997 Identification of lactosylated sites by trypsinolysis and Tandem MS indicate that, although the glycosylation reaction was non-specific and potentially involved all the reactive sites (alpha- and epsilon-amino groups), beta-LG appeared to have at least two populations of lysine with the distinct ability to react with lactose. Lactose 319-326 beta-lactoglobulin Bos taurus 219-226 9240451-4 1997 These results underline the structural heterogeneity of beta-LG glycoforms, with respect to the number of lactose linked per molecule and to the binding sites involved, which could affect the biological function of beta-LG. Lactose 106-113 beta-lactoglobulin Bos taurus 56-63 9240451-4 1997 These results underline the structural heterogeneity of beta-LG glycoforms, with respect to the number of lactose linked per molecule and to the binding sites involved, which could affect the biological function of beta-LG. Lactose 106-113 beta-lactoglobulin Bos taurus 215-222 2350400-3 1990 Ten percent lactose-feeding resulted in decreased tissue conductance and significantly reduced (-58%, P less than 0.05) beta-LG transport across rat small intestinal mucosa. Lactose 12-19 beta-lactoglobulin Bos taurus 120-127 32635246-4 2020 As a function of heating, beta-lactoglobulin was shown to become increasingly prone to denaturation, aggregation, and lactose conjugation. Lactose 118-125 beta-lactoglobulin Bos taurus 26-44 33559978-4 2021 METHODS AND RESULTS: The binding and uptake of BLG from raw cow milk and heated either alone (BLG-H) or with lactose/glucose (BLG-Lac and BLG-Glu) to the receptors present on APCs were analysed by ELISA and cell-binding assays. Lactose 109-116 beta-lactoglobulin Bos taurus 47-50 32057430-2 2020 The IgG/IgE binding capacity and structural characteristics of beta-LG after spray drying in the presence or absence of alpha-lactose at 120 and 180 C were investigated by ELISA and mass spectrometry. Lactose 120-133 beta-lactoglobulin Bos taurus 63-70 32057430-5 2020 When alpha-lactose was also present, 7 lysine side-chains in beta-LG were modified by glycation and the IgG/IgE binding capacity was further decreased. Lactose 5-18 beta-lactoglobulin Bos taurus 61-68 31242665-3 2019 BLG was heated under dry conditions (water activity < 0.7) and wet conditions (in phosphate buffer at pH 7.4) at low temperature (<73 C) and high temperatures (>90 C) in the presence or absence of the milk sugar lactose. Lactose 223-230 beta-lactoglobulin Bos taurus 0-3 28490136-3 2017 Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Lactose 47-54 beta-lactoglobulin Bos taurus 20-23 26923048-4 2016 Heating in the presence of lactose resulted in significant Maillard modification (both lactosylation and carboxymethylation) to both bovine lactoferrin and beta-lactoglobulin. Lactose 27-34 beta-lactoglobulin Bos taurus 156-174