PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21997288-1 2012 Continuous 295 nm excitation of whey protein bovine apo-alpha-lactalbumin (apo-bLA) results in an increase of tryptophan fluorescence emission intensity, in a progressive red-shift of tryptophan fluorescence emission, and breakage of disulphide bridges (SS), yielding free thiol groups. Tryptophan 110-120 lactalbumin alpha Bos taurus 56-73 29331461-7 2018 Tryptophan fluorescence quenching measurements indicated that alpha-LA has one binding site at pH 7.4 but acquires an additional binding site when the pH is lowered to pH 2 to 4. Tryptophan 0-10 lactalbumin alpha Bos taurus 62-70 21997288-1 2012 Continuous 295 nm excitation of whey protein bovine apo-alpha-lactalbumin (apo-bLA) results in an increase of tryptophan fluorescence emission intensity, in a progressive red-shift of tryptophan fluorescence emission, and breakage of disulphide bridges (SS), yielding free thiol groups. Tryptophan 184-194 lactalbumin alpha Bos taurus 56-73 20372885-0 2010 Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach. Tryptophan 10-20 lactalbumin alpha Bos taurus 77-94 4084580-1 1985 The proton nuclear Overhauser effects of bovine alpha-lactalbumin were studied at 200 MHz by irradiation of an upfield ring current shifted methylene at -2.45 ppm (assigned to Ile-95) and two aromatic protons, Tyr-103 (8.36 ppm) and Trp-60 (5.85 ppm). Tryptophan 233-236 lactalbumin alpha Bos taurus 48-65 20346348-0 2010 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. Tryptophan 29-40 lactalbumin alpha Bos taurus 79-96 14991658-8 2004 It is observed that two of four tryptophans are exposed to the solvent in the HFIP induced molten globule state of alpha-lactalbumin compared to four in the 8.5M urea induced denatured state of the protein. Tryptophan 32-43 lactalbumin alpha Bos taurus 115-132 3114129-0 1987 Effect of tryptophan modification in cow and buffalo alpha-lactalbumin on galactosyltransferase activity--modification by 2-nitrophenyl sulphenyl chloride and 2-hydroxy 5-nitrobenzyl bromide. Tryptophan 10-20 lactalbumin alpha Bos taurus 53-70 10837296-0 2000 The bovine protein alpha-lactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress. Tryptophan 67-77 lactalbumin alpha Bos taurus 19-36 10837296-4 2000 OBJECTIVE: We tested whether alpha-lactalbumin, a whey protein with a high tryptophan content, may increase the plasma Trp-LNAA ratio and reduce depressive mood and cortisol concentrations in stress-vulnerable subjects under acute stress. Tryptophan 75-85 lactalbumin alpha Bos taurus 29-46 10837296-4 2000 OBJECTIVE: We tested whether alpha-lactalbumin, a whey protein with a high tryptophan content, may increase the plasma Trp-LNAA ratio and reduce depressive mood and cortisol concentrations in stress-vulnerable subjects under acute stress. Tryptophan 119-122 lactalbumin alpha Bos taurus 29-46 10837296-9 2000 RESULTS: The plasma Trp-LNAA ratio was 48% higher after the alpha-lactalbumin diet than after the casein diet (P = 0.0001). Tryptophan 20-23 lactalbumin alpha Bos taurus 60-77 9388223-2 1997 An intrinsic fluorescence titration of various alpha-LA forms with 5-doxylstearic acid causes first an increase and then a decrease in emission intensity with concomitant shifts in tryptophan emission wavelength. Tryptophan 181-191 lactalbumin alpha Bos taurus 47-55 8563628-8 1995 This transition was interpreted as being a result of a change of the alpha-LA tertiary structure, which resulted in a loss of asymmetry of the environment of both the tryptophan residues and the ANS hydrophobic binding sites. Tryptophan 167-177 lactalbumin alpha Bos taurus 69-77 3370298-0 1988 Hydrogen exchange of the tryptophan residues in bovine alpha-lactalbumin studied by UV spectroscopy. Tryptophan 25-35 lactalbumin alpha Bos taurus 55-72 6871261-1 1983 Lifetimes of phenylalanine, tyrosine and tryptophan self-fluorescence of three Ca2+-binding proteins (parvalbumins pI 4.47 and 3.95 and bovine alpha-lactalbumin) in the Ca2+-saturated state and without Ca2+ were measured on a device functioning in a channel of synchrotron radiation of the Lebedev Physical Institute electron accelerator C-60 with a single photon counting system. Tryptophan 41-51 lactalbumin alpha Bos taurus 143-160 6871261-9 1983 It is concluded that in Ca2+-saturated alpha-lactalbumin some tryptophane residues are located near the quenching groups (dynamic quenching), most likely the disulfide bridges. Tryptophan 62-73 lactalbumin alpha Bos taurus 39-56 410450-6 1977 As with bovine alpha-lactalbumin, at pH 2.7, 2-hydroxy-5-nitrobenzyl bromide is specific for tryptophan but at pH 7 His-32 also reacts. Tryptophan 93-103 lactalbumin alpha Bos taurus 15-32 963237-0 1976 Hydrogen-deuterium exchange of the tryptophan residues in bovine alpha-lactalbumin. Tryptophan 35-45 lactalbumin alpha Bos taurus 65-82 1004498-1 1976 The deuteration of the tryptophan residues of hen egg white lysozyme, bovine alpha-lactalbumin and bovine beta-lactoglobulin in d-TFA has been studied by PMR spectroscopy. Tryptophan 23-33 lactalbumin alpha Bos taurus 77-94 809437-1 1975 Reaction of alpha-lactalbumin at pH 7 in aqueous solution with either 2-hydroxy-5-nitrobenzylbromide or N-bromosuccinimide yields derivatives in which only 2 of the 4 tryptophan residues are modified. Tryptophan 167-177 lactalbumin alpha Bos taurus 12-29 809437-4 1975 The fluorescence of alpha-lactalbumin modified to varying extents with N-bromosuccinimide indicates that tryptophan 118 is exposed to solvent whereas tryptophan 26 is in a more hydrophobic environment. Tryptophan 105-115 lactalbumin alpha Bos taurus 20-37 809437-4 1975 The fluorescence of alpha-lactalbumin modified to varying extents with N-bromosuccinimide indicates that tryptophan 118 is exposed to solvent whereas tryptophan 26 is in a more hydrophobic environment. Tryptophan 150-160 lactalbumin alpha Bos taurus 20-37 809437-5 1975 The chemical reactivities and fluorescence properties of tryptophans 26 and 118 are consistent with the proposed conformations of alpha-lactalbumin based on its similarity with egg white lysozyme. Tryptophan 57-68 lactalbumin alpha Bos taurus 130-147 5063246-0 1972 The modification of the tryptophan residues of bovine alpha-lactalbumin with 2-hydroxy-5-nitrobenzyl bromide and with dimethyl(2-hydroxy-5-nitrobenzyl)sulphonium bromide. Tryptophan 24-34 lactalbumin alpha Bos taurus 54-71 238614-7 1975 The results support the suggestion that the two tryptophan residues found in the active site cleft of alpha-lactalbumin may be largely responsible for its luminescence. Tryptophan 48-58 lactalbumin alpha Bos taurus 102-119 236187-6 1975 Some changes in the fluorescence spectrum (peak shifting towards longer wavelength) was observed for bovine alpha-lactalbumin and appeared to be due to alteration of the environment of the tryptophan side-chains in the protein upon coupling to the agarose gel. Tryptophan 189-199 lactalbumin alpha Bos taurus 108-125 4249929-0 1970 Differences in tryptophan exposure between chicken egg-white lysozyme and bovine alpha-lactalbumin. Tryptophan 15-25 lactalbumin alpha Bos taurus 81-98 30527978-9 2019 The whey protein alpha-lactalbumin showed the highest antioxidant properties post-SGID (oxygen radical absorbance capacity = 1,825.94 +- 50.21 mumol of Trolox equivalents/g of powder) of the 4 major whey proteins tested with the release of the highest amount of the antioxidant AA tryptophan, 6.955 mumol of tryptophan/g of protein. Tryptophan 281-291 lactalbumin alpha Bos taurus 17-34 30527978-9 2019 The whey protein alpha-lactalbumin showed the highest antioxidant properties post-SGID (oxygen radical absorbance capacity = 1,825.94 +- 50.21 mumol of Trolox equivalents/g of powder) of the 4 major whey proteins tested with the release of the highest amount of the antioxidant AA tryptophan, 6.955 mumol of tryptophan/g of protein. Tryptophan 308-318 lactalbumin alpha Bos taurus 17-34