PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34461523-3 2022 The change in structure, stability and rate of fibril formation of aggregation-prone partially-unfolded states of lysozyme (Lyz) and alpha-lactalbumin (ALA) in the presence of different sizes of polyethylene glycol (PEG) is examined using spectroscopic methods. Polyethylene Glycols 195-214 lactalbumin alpha Homo sapiens 133-150 8720849-3 1995 When dissolving whey powder in the salt-rich phase of the system, alpha-lactalbumin was extracted to the polyethylene-glycol-rich phase, whereas beta-lactoglobulin predominantly remained in the bottom phase, making the process suitable for removal of the major allergen beta-lactoglobulin. Polyethylene Glycols 105-124 lactalbumin alpha Homo sapiens 66-83 9544802-1 1998 The electrophoretic behavior of alpha-lactalbumin and beta-lactoglobulins (A and B) in the presence of non-ionic surfactants was studied by capillary electrophoresis (CE), using a poly(ethylene glycol) coated capillary column. Polyethylene Glycols 180-201 lactalbumin alpha Homo sapiens 32-49 34461523-3 2022 The change in structure, stability and rate of fibril formation of aggregation-prone partially-unfolded states of lysozyme (Lyz) and alpha-lactalbumin (ALA) in the presence of different sizes of polyethylene glycol (PEG) is examined using spectroscopic methods. Polyethylene Glycols 216-219 lactalbumin alpha Homo sapiens 133-150 21404256-3 2011 Data were obtained with alpha-lactalbumin that was PEGylated with a 20 kDa activated PEG, with the ultrafiltration performed over a range of pH and ionic strength using both unmodified and negatively charged composite regenerated cellulose membranes. Polyethylene Glycols 51-54 lactalbumin alpha Homo sapiens 24-41 34726117-0 2021 PEG mediated destabilization of holo alpha-lactalbumin probed by in silico and in vitro studies: deviation from excluded volume effect. Polyethylene Glycols 0-3 lactalbumin alpha Homo sapiens 37-54 32885978-2 2020 Here, we demonstrate that alpha-lactalbumin/polyethylene oxide (ALA/PEO) electrospun nanofibers constitute an efficient oromucosal delivery system for fast-onset nicotine delivery of high relevance for acute dosing NRT applications. Polyethylene Glycols 68-71 lactalbumin alpha Homo sapiens 26-43 26593565-2 2016 By adding a non-ionic poly(ethylene glycol) (PEG) chain onto the reducing end of CMD, forming carboxymethyl-dextran-block-poly(ethylene glycol) (CMD-b-PEG), the PEG block was hypothesized to reduce interactions with alpha-lac and promote formation of a micelle-like complex structure. Polyethylene Glycols 45-48 lactalbumin alpha Homo sapiens 216-225 23436792-4 2013 The transmission of the pegylated alpha-lactalbumin, PEG, and alpha-lactalbumin all increase with increasing PEG concentration due to the increase in the solute partition coefficient arising from unfavorable intermolecular interactions in the bulk solution. Polyethylene Glycols 109-112 lactalbumin alpha Homo sapiens 34-51 23436792-4 2013 The transmission of the pegylated alpha-lactalbumin, PEG, and alpha-lactalbumin all increase with increasing PEG concentration due to the increase in the solute partition coefficient arising from unfavorable intermolecular interactions in the bulk solution. Polyethylene Glycols 109-112 lactalbumin alpha Homo sapiens 62-79 22735492-3 2012 Here we report that the crowding agents Ficoll 70, dextran 70, and polyethylene glycol (PEG) 2000 have different effects on the structural stability of human alpha-lactalbumin (HLA) represented by the transition to a molten globule state: dextran 70 dramatically enhances the thermal stability of Ca(2+)-depleted HLA (apo-HLA) and Ficoll 70 enhances the thermal stability of apo-HLA to some extent, while PEG 2000 significantly decreases the thermal stability of apo-HLA. Polyethylene Glycols 67-86 lactalbumin alpha Homo sapiens 158-175 22735492-3 2012 Here we report that the crowding agents Ficoll 70, dextran 70, and polyethylene glycol (PEG) 2000 have different effects on the structural stability of human alpha-lactalbumin (HLA) represented by the transition to a molten globule state: dextran 70 dramatically enhances the thermal stability of Ca(2+)-depleted HLA (apo-HLA) and Ficoll 70 enhances the thermal stability of apo-HLA to some extent, while PEG 2000 significantly decreases the thermal stability of apo-HLA. Polyethylene Glycols 88-91 lactalbumin alpha Homo sapiens 158-175 22735492-3 2012 Here we report that the crowding agents Ficoll 70, dextran 70, and polyethylene glycol (PEG) 2000 have different effects on the structural stability of human alpha-lactalbumin (HLA) represented by the transition to a molten globule state: dextran 70 dramatically enhances the thermal stability of Ca(2+)-depleted HLA (apo-HLA) and Ficoll 70 enhances the thermal stability of apo-HLA to some extent, while PEG 2000 significantly decreases the thermal stability of apo-HLA. Polyethylene Glycols 405-408 lactalbumin alpha Homo sapiens 158-175 21621485-3 2011 It was found that alpha-la and Gmp partitioned to the top phase rich in PEG, whereas beta-lg partitioned to the bottom phase rich in salt. Polyethylene Glycols 72-75 lactalbumin alpha Homo sapiens 18-26 20149779-1 2010 A microchip electrophoretic method was applied to monitor and characterize the covalent attachment of poly(ethylene glycol) (PEGylation) of two proteins, alpha-lactalbumin and bovine serum albumin, using several poly(ethylene glycol) (PEG) derivatives with molecular weights from 1 to 20 kDa. Polyethylene Glycols 102-123 lactalbumin alpha Homo sapiens 154-171 20149779-1 2010 A microchip electrophoretic method was applied to monitor and characterize the covalent attachment of poly(ethylene glycol) (PEGylation) of two proteins, alpha-lactalbumin and bovine serum albumin, using several poly(ethylene glycol) (PEG) derivatives with molecular weights from 1 to 20 kDa. Polyethylene Glycols 212-233 lactalbumin alpha Homo sapiens 154-171 20149779-1 2010 A microchip electrophoretic method was applied to monitor and characterize the covalent attachment of poly(ethylene glycol) (PEGylation) of two proteins, alpha-lactalbumin and bovine serum albumin, using several poly(ethylene glycol) (PEG) derivatives with molecular weights from 1 to 20 kDa. Polyethylene Glycols 125-128 lactalbumin alpha Homo sapiens 154-171