PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23395255-6 2013 alpha-Lactalbumin increased plasma tryptophan (3-fold) and the tryptophan ratio (50%); starch did not change either tryptophan variable, while gluten caused a modest (25%) and zein a large reduction (50%) in plasma tryptophan. Tryptophan 35-45 lactalbumin alpha Homo sapiens 0-17 23395255-6 2013 alpha-Lactalbumin increased plasma tryptophan (3-fold) and the tryptophan ratio (50%); starch did not change either tryptophan variable, while gluten caused a modest (25%) and zein a large reduction (50%) in plasma tryptophan. Tryptophan 63-73 lactalbumin alpha Homo sapiens 0-17 23395255-6 2013 alpha-Lactalbumin increased plasma tryptophan (3-fold) and the tryptophan ratio (50%); starch did not change either tryptophan variable, while gluten caused a modest (25%) and zein a large reduction (50%) in plasma tryptophan. Tryptophan 63-73 lactalbumin alpha Homo sapiens 0-17 23395255-6 2013 alpha-Lactalbumin increased plasma tryptophan (3-fold) and the tryptophan ratio (50%); starch did not change either tryptophan variable, while gluten caused a modest (25%) and zein a large reduction (50%) in plasma tryptophan. Tryptophan 63-73 lactalbumin alpha Homo sapiens 0-17 23395255-8 2013 The maximal difference in the tryptophan ratio occurred between alpha-lactalbumin and zein and was large (~3-fold). Tryptophan 30-40 lactalbumin alpha Homo sapiens 64-81 18044829-6 2007 Changes at the tertiary protein structure level were observed after photo-oxidation of the globular proteins, where tryptophan fluorescence emission indicated unfolding of alpha-lactalbumin and beta-lactoglobulin, whereas lactoferrin achieved a more compact tertiary structure. Tryptophan 116-126 lactalbumin alpha Homo sapiens 172-189 19017422-8 2009 TRP concentrations were higher after alpha-lactalbumin than after gelatin with or without TRP from t = 0-100 min, whereas from t = 100-240 min, TRP concentrations were lower after gelatin than after alpha-lactalbumin and gelatin+TRP. Tryptophan 0-3 lactalbumin alpha Homo sapiens 37-54 18648776-2 2008 Since the production of serotonin is limited by the availability of its plasma dietary amino acid precursor tryptophan (TRP), the beneficial effects of tryptophan-rich alpha-lactalbumin whey protein (ALAC) have recently been studied. Tryptophan 152-162 lactalbumin alpha Homo sapiens 168-185 21335989-3 2011 alpha-Lactalbumin was first isolated to provide a good source of tryptophan, often the first limiting amino acid in infant formulas, but has then been shown to be digested into smaller peptides with antimicrobial and prebiotic activities, immunostimulatory effect and acting as enhancers of mineral absorption. Tryptophan 65-75 lactalbumin alpha Homo sapiens 0-17 16176613-2 2005 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. Tryptophan 62-72 lactalbumin alpha Homo sapiens 21-38 16174675-2 2006 A diet rich in alpha-lactalbumin protein has been found to increase the ratio tryptophan /large neutral amino acids (Trp/SigmaLNAA), and to improve cognitive functioning in individuals with high neuroticism scores. Tryptophan 78-88 lactalbumin alpha Homo sapiens 15-32 16174675-2 2006 A diet rich in alpha-lactalbumin protein has been found to increase the ratio tryptophan /large neutral amino acids (Trp/SigmaLNAA), and to improve cognitive functioning in individuals with high neuroticism scores. Tryptophan 117-120 lactalbumin alpha Homo sapiens 15-32 17606474-5 2007 All subjects performed the attention switch task in the morning following breakfast containing either tryptophan-rich alpha-lactalbumin (4.8 g/100 g TRP) or placebo protein (1.4 g/100 g TRP). Tryptophan 102-112 lactalbumin alpha Homo sapiens 118-135 17446205-2 2007 Recent studies suggest that alpha-lactalbumin, a whey-derived protein with a relatively high TRP content, increases plasma TRP and produces endocrine and cognitive changes consistent with facilitation of brain 5-HT function. Tryptophan 93-96 lactalbumin alpha Homo sapiens 28-45 17446205-2 2007 Recent studies suggest that alpha-lactalbumin, a whey-derived protein with a relatively high TRP content, increases plasma TRP and produces endocrine and cognitive changes consistent with facilitation of brain 5-HT function. Tryptophan 123-126 lactalbumin alpha Homo sapiens 28-45 17446205-4 2007 Relative to a casein-derived control protein, alpha-lactalbumin increased plasma TRP and the ratio of TRP to neutral amino acids. Tryptophan 81-84 lactalbumin alpha Homo sapiens 46-63 17446205-4 2007 Relative to a casein-derived control protein, alpha-lactalbumin increased plasma TRP and the ratio of TRP to neutral amino acids. Tryptophan 102-105 lactalbumin alpha Homo sapiens 46-63 17446205-6 2007 The results suggest that alpha-lactalbumin produces a relatively modest increase in TRP availability which may not be sufficient to produce the changes in emotional processing seen with administration of pure TRP in healthy subjects. Tryptophan 84-87 lactalbumin alpha Homo sapiens 25-42 16176613-8 2005 Although the alpha-lactalbumin diet led to the expected rises in tryptophan and tryptophan:large neutral amino acids ratio, only minimal effects were found on mood and cortisol response to experimental stress. Tryptophan 65-75 lactalbumin alpha Homo sapiens 13-30 16176613-8 2005 Although the alpha-lactalbumin diet led to the expected rises in tryptophan and tryptophan:large neutral amino acids ratio, only minimal effects were found on mood and cortisol response to experimental stress. Tryptophan 80-90 lactalbumin alpha Homo sapiens 13-30 15883425-0 2005 Evening intake of alpha-lactalbumin increases plasma tryptophan availability and improves morning alertness and brain measures of attention. Tryptophan 53-63 lactalbumin alpha Homo sapiens 18-35 15883425-3 2005 OBJECTIVE: We tested whether evening consumption of alpha-lactalbumin protein with an enriched tryptophan content of 4.8 g/100 g increases plasma Trp:LNAA and improves alertness and performance on the morning after sleep, particularly in subjects with sleep complaints. Tryptophan 95-105 lactalbumin alpha Homo sapiens 52-69 15883425-3 2005 OBJECTIVE: We tested whether evening consumption of alpha-lactalbumin protein with an enriched tryptophan content of 4.8 g/100 g increases plasma Trp:LNAA and improves alertness and performance on the morning after sleep, particularly in subjects with sleep complaints. Tryptophan 146-149 lactalbumin alpha Homo sapiens 52-69 15883425-5 2005 The subjects slept at the laboratory for 2 separate nights so that morning performance could be evaluated after an evening diet containing either tryptophan-rich alpha-lactalbumin or tryptophan-low placebo protein. Tryptophan 146-156 lactalbumin alpha Homo sapiens 162-179 15883425-8 2005 RESULTS: Evening alpha-lactalbumin intake caused a 130% increase in Trp:LNAA before bedtime (P = 0.0001) and modestly but significantly reduced sleepiness (P = 0.013) and improved brain-sustained attention processes (P = 0.002) the following morning. Tryptophan 68-71 lactalbumin alpha Homo sapiens 17-34 15178151-0 2004 Alpha-lactalbumin combined with a regular diet increases plasma Trp-LNAA ratio. Tryptophan 64-67 lactalbumin alpha Homo sapiens 0-17 12812154-6 2003 alpha-Lactalbumin is rich in tryptophan, which is typically the limiting amino acid in formula, and as a result, formulas have been developed with lower protein but higher tryptophan concentrations. Tryptophan 29-39 lactalbumin alpha Homo sapiens 0-17 15178151-13 2004 We conclude that an alpha-lactalbumin-enriched supplement combined with a regular diet increases plasma Trp-LNAA ratio and may influence serum prolactin, but we could not demonstrate effects on appetite, food intake, macronutrient preference and mood. Tryptophan 104-107 lactalbumin alpha Homo sapiens 20-37 12812154-6 2003 alpha-Lactalbumin is rich in tryptophan, which is typically the limiting amino acid in formula, and as a result, formulas have been developed with lower protein but higher tryptophan concentrations. Tryptophan 172-182 lactalbumin alpha Homo sapiens 0-17 12784209-1 2003 Prolonged exposure of Ca(2+)-loaded or Ca(2+)-depleted human alpha-lactalbumin to ultraviolet light (270-290 nm, 1 mW/cm(2), for 2 to 4 h) results in a 10-nm red shift of its tryptophan fluorescence spectrum. Tryptophan 175-185 lactalbumin alpha Homo sapiens 61-78 12784209-5 2003 It is assumed that the UV excitation of tryptophan residue(s) in alpha-lactalbumin is followed by a transfer of electrons to the Sbond;S bonds, resulting in their reduction. Tryptophan 40-50 lactalbumin alpha Homo sapiens 65-82 1815583-2 1991 The intrinsic tryptophan fluorescence spectrum of Ca(II)-loaded alpha-lactalbumin is insensitive to Zn(II) binding to the strong cation binding sites (Zn:protein ratios up to 20), yet the thermal denaturation transition, as detected by intrinsic fluorescence, is shifted toward lower temperatures. Tryptophan 14-24 lactalbumin alpha Homo sapiens 64-81 12036812-5 2002 OBJECTIVE: We tested whether alpha-lactalbumin, a whey protein with a high tryptophan content, would increase the plasma Trp-LNAA ratio and improve cognitive performance in high stress- vulnerable subjects. Tryptophan 121-124 lactalbumin alpha Homo sapiens 29-46 12036812-9 2002 RESULTS: A significantly greater increase in the plasma Trp-LNAA ratio after consumption of the alpha-lactalbumin diet than after the control diet (P = 0.0001) was observed; memory scanning improved significantly only in the high stress-vulnerable subjects (P = 0.019). Tryptophan 56-59 lactalbumin alpha Homo sapiens 96-113 12036812-10 2002 CONCLUSION: Because an increase in the plasma Trp-LNAA ratio is considered to be an indirect indication of increased brain serotonin function, the results suggest that dietary protein rich in alpha-lactalbumin improves cognitive performance in stress-vulnerable subjects via increased brain tryptophan and serotonin activities. Tryptophan 46-49 lactalbumin alpha Homo sapiens 192-209 12036812-10 2002 CONCLUSION: Because an increase in the plasma Trp-LNAA ratio is considered to be an indirect indication of increased brain serotonin function, the results suggest that dietary protein rich in alpha-lactalbumin improves cognitive performance in stress-vulnerable subjects via increased brain tryptophan and serotonin activities. Tryptophan 291-301 lactalbumin alpha Homo sapiens 192-209 11401570-0 2001 Structure and dynamics of the alpha-lactalbumin molten globule: fluorescence studies using proteins containing a single tryptophan residue. Tryptophan 120-130 lactalbumin alpha Homo sapiens 30-47 11401570-1 2001 The fluorescence properties of three variants of alpha-lactalbumin (alpha-LA) containing a single tryptophan residue were investigated under native, molten globule, and unfolded conditions. Tryptophan 98-108 lactalbumin alpha Homo sapiens 49-66 11401570-1 2001 The fluorescence properties of three variants of alpha-lactalbumin (alpha-LA) containing a single tryptophan residue were investigated under native, molten globule, and unfolded conditions. Tryptophan 98-108 lactalbumin alpha Homo sapiens 68-76 27414133-0 2000 Dose-Dependent Effect of alpha-Lactalbumin in Combination with Two Different Doses of Glucose on the Plasma Trp/LNAA Ratio. Tryptophan 108-111 lactalbumin alpha Homo sapiens 25-42 27414133-3 2000 In the present study, we investigated the time- and dose dependent effects of alpha-lactalbumin enriched whey protein with a high tryptophan content in combination with two doses of glucose on plasma Trp/LNAA. Tryptophan 200-203 lactalbumin alpha Homo sapiens 78-95 27414133-7 2000 Different doses interacted with time-dependent changes in plasma Trp/LNAA [P < 0.0001] such that the most prolonged increase was found with 20 g alpha-lactalbumin [P < 0.0001]. Tryptophan 65-68 lactalbumin alpha Homo sapiens 148-165 10512721-2 1999 The refolding reactions induced by stopped-flow pH jumps were monitored by alpha-lactalbumin tryptophan fluorescence. Tryptophan 93-103 lactalbumin alpha Homo sapiens 75-92 1290937-3 1992 Side-group ROA features also appear, with tryptophan particularly prominent in lysozyme and alpha-lactalbumin. Tryptophan 42-52 lactalbumin alpha Homo sapiens 92-109 12036812-0 2002 Whey protein rich in alpha-lactalbumin increases the ratio of plasma tryptophan to the sum of the other large neutral amino acids and improves cognitive performance in stress-vulnerable subjects. Tryptophan 69-79 lactalbumin alpha Homo sapiens 21-38 12036812-5 2002 OBJECTIVE: We tested whether alpha-lactalbumin, a whey protein with a high tryptophan content, would increase the plasma Trp-LNAA ratio and improve cognitive performance in high stress- vulnerable subjects. Tryptophan 75-85 lactalbumin alpha Homo sapiens 29-46 10721122-4 1999 alpha-lactalbumin enriched, protein-reduced formulas adapted to 2.2% Trp were shown to be capable of producing Trp serum values that did not differ from those in breast-fed infants. Tryptophan 69-72 lactalbumin alpha Homo sapiens 0-17 10721122-4 1999 alpha-lactalbumin enriched, protein-reduced formulas adapted to 2.2% Trp were shown to be capable of producing Trp serum values that did not differ from those in breast-fed infants. Tryptophan 111-114 lactalbumin alpha Homo sapiens 0-17 3349046-7 1988 Characterization of four Trp"s in alpha-lactalbumin shows that the two outer Trp"s are moderately H bonded to solvent water and closely surrounded by aliphatic side chains while the inner two are not H bonded nor closely surrounded by aliphatic side chains. Tryptophan 25-28 lactalbumin alpha Homo sapiens 34-51 2059662-5 1991 The interaction of apo-alpha-lactalbumin with melittin causes some changes in the environment of its aromatic amino acid residues and drastically alters the conformation of melittin, increasing its alpha-helical content but leaving its single tryptophan residue accessible to water. Tryptophan 243-253 lactalbumin alpha Homo sapiens 23-40 2605208-0 1989 Hydrogen exchange of the tryptophan residues in bovine, goat, guinea pig, and human alpha-lactalbumin. Tryptophan 25-35 lactalbumin alpha Homo sapiens 84-101 2605208-1 1989 Hydrogen exchange of the individual tryptophan residues of bovine, goat, guinea pig, and human alpha-lactalbumin has been studied by both ultraviolet and NMR spectra. Tryptophan 36-46 lactalbumin alpha Homo sapiens 95-112 2605208-2 1989 The assignment of the slowly exchanging imino proton resonances to the tryptophan residues (Trp26 and Trp60) was obtained by comparison of the nuclear Overhauser effect difference spectra of bovine, guinea pig, and human alpha-lactalbumin. Tryptophan 71-81 lactalbumin alpha Homo sapiens 221-238 2605208-3 1989 Taking account of the thermal unfolding of each alpha-lactalbumin, the hydrogen exchange rates of the individual tryptophan residues are analyzed. Tryptophan 113-123 lactalbumin alpha Homo sapiens 48-65 2605208-8 1989 Trp104 and Trp118 of alpha-lactalbumin exchange through the low activation energy process, and the reaction rates are affected by the local structural differences around the tryptophan residues among these proteins. Tryptophan 174-184 lactalbumin alpha Homo sapiens 21-38 2716061-2 1989 The reversible unfolding and refolding kinetics of alpha-lactalbumin induced by concentration jump of guanidine hydrochloride were measured at pH 7.0 and 25 degrees C using tryptophan absorption at 292 nm, with varying concentrations of the denaturant and free Ca2+. Tryptophan 173-183 lactalbumin alpha Homo sapiens 51-68 3416039-0 1988 Environment of tryptophan residues in various conformational states of alpha-lactalbumin studied by time-resolved and steady-state fluorescence spectroscopy. Tryptophan 15-25 lactalbumin alpha Homo sapiens 71-88 3416039-1 1988 Decay curves for tryptophan fluorescence of bovine and human alpha-lactalbumin in different states (metal-free and Ca2+ or Mg2+-loaded states of the native and thermally denatured proteins) have been measured at different wavelengths. Tryptophan 17-27 lactalbumin alpha Homo sapiens 61-78 3416039-3 1988 The results suggests that the red shift of the fluorescence spectrum of alpha-lactalbumin caused by release of the bound Ca2+ or thermal denaturation is due to changes in the environment of all emitting tryptophan residues. Tryptophan 203-213 lactalbumin alpha Homo sapiens 72-89 3349046-7 1988 Characterization of four Trp"s in alpha-lactalbumin shows that the two outer Trp"s are moderately H bonded to solvent water and closely surrounded by aliphatic side chains while the inner two are not H bonded nor closely surrounded by aliphatic side chains. Tryptophan 77-80 lactalbumin alpha Homo sapiens 34-51 6788764-8 1981 The interaction of galactosyltransferase and alpha-lactalbumin produces difference spectra characteristic of tryptophan and does not affect the difference spectra of galactosyltransferase produced by the interaction with UDP and GlcNAc. Tryptophan 109-119 lactalbumin alpha Homo sapiens 45-62 3763824-5 1986 The peptides L-II (aa 13-105) and alpha-I (aa 1-90) from lysozyme and alpha-lactalbumin, respectively, showed Trp residues with different degree of exposure, whereas the smaller fragments, L-III (aa 106-129) and alpha-II (aa 91-123), had all their Trp residues exposed to the solvent. Tryptophan 110-113 lactalbumin alpha Homo sapiens 70-87 415861-1 1978 His-32 of bovine or human alpha-lactalbumin reacts with the tryptophan reagent 2-hydroxy-5-nitrobenzyl bromide at pH 7. Tryptophan 60-70 lactalbumin alpha Homo sapiens 26-43 5485915-0 1970 Reactivities of the tryptophan residues of alpha-lactalbumin and lysozyme to 2-hydroxy-5-nitrobenzyl bromide. Tryptophan 20-30 lactalbumin alpha Homo sapiens 43-60 24620-0 1978 Environment of tryptophan residues in alpha-lactalbumin. Tryptophan 15-25 lactalbumin alpha Homo sapiens 38-55 812700-7 1975 In sharp contrast the additional nitration of a single tryptophan residue totally abolished the specifying activity of alpha-lactalbumin. Tryptophan 55-65 lactalbumin alpha Homo sapiens 119-136 410450-0 1977 On the reactivities of the tryptophan residues of human alpha-lactalbumin to 2-hydroxy-5-nitrobenzyl bromide. Tryptophan 27-37 lactalbumin alpha Homo sapiens 56-73 410450-1 1977 The reaction of human alpha-lactalbumin with the tryptophan reagent 2-hydroxy-5-nitrobenzyl bromide has been studied. Tryptophan 49-59 lactalbumin alpha Homo sapiens 22-39 410450-3 1977 Trp-60 of human alpha-lactalbumin is much more reactive than Trp-60 of bovine alpha-lactalbumin (Barman, T. E. (1972) Biochim. Tryptophan 0-3 lactalbumin alpha Homo sapiens 16-33 25823693-4 2015 The aims were to investigate the effect of oral l-tryptophan and alpha-lactalbumin, a protein with high tryptophan concentration, on total and free tryptophan levels in breast milk and plasma, and to compare free tryptophan levels in breast milk with those in common infant formulas. Tryptophan 104-114 lactalbumin alpha Homo sapiens 65-82 33784543-6 2021 Both synchronous and 3D fluorescence analysis suggested that the microenvironment around tryptophan residues had changed, which coincided with the result of molecular docking that tryptophan residue of alpha-lactalbumin contributed significantly to hydrogen bonding. Tryptophan 89-99 lactalbumin alpha Homo sapiens 202-219 33784543-6 2021 Both synchronous and 3D fluorescence analysis suggested that the microenvironment around tryptophan residues had changed, which coincided with the result of molecular docking that tryptophan residue of alpha-lactalbumin contributed significantly to hydrogen bonding. Tryptophan 180-190 lactalbumin alpha Homo sapiens 202-219 32698123-1 2020 We tested the hypothesis that presleep consumption of alpha-lactalbumin (LA), a fraction of whey with a high abundance of tryptophan, would improve indices of sleep quality and time-trial (TT) performance in cyclists relative to an isonitrogenous collagen peptide (CP) supplement lacking tryptophan. Tryptophan 122-132 lactalbumin alpha Homo sapiens 54-71 32698123-1 2020 We tested the hypothesis that presleep consumption of alpha-lactalbumin (LA), a fraction of whey with a high abundance of tryptophan, would improve indices of sleep quality and time-trial (TT) performance in cyclists relative to an isonitrogenous collagen peptide (CP) supplement lacking tryptophan. Tryptophan 288-298 lactalbumin alpha Homo sapiens 54-71 28796377-0 2017 Tryptophan and Cysteine Oxidation Products Dominate in alpha-Lactalbumin-Derived Peptides Analyzed with LC-MSn. Tryptophan 0-10 lactalbumin alpha Homo sapiens 55-72 31895298-3 2020 The aim of this study was to determine whether supplementation with alpha-Lactalbumin (LA), with high leucine and tryptophan contents, would improve responses to short periods of intensified aerobic training compared to supplementation with an isonitrogenous quantity of collagen peptides (CP). Tryptophan 114-124 lactalbumin alpha Homo sapiens 68-85 25823693-4 2015 The aims were to investigate the effect of oral l-tryptophan and alpha-lactalbumin, a protein with high tryptophan concentration, on total and free tryptophan levels in breast milk and plasma, and to compare free tryptophan levels in breast milk with those in common infant formulas. Tryptophan 104-114 lactalbumin alpha Homo sapiens 65-82 25823693-8 2015 Both l-tryptophan and alpha-lactalbumin were associated with greater free tryptophan levels in breast milk (rANOVA, group effect: p<0.001) (representing 2% of total tryptophan), but these concentrations were within the range of commonly used infant formulas. Tryptophan 74-84 lactalbumin alpha Homo sapiens 22-39 25586395-5 2015 With protein-based formulations, alpha-lactalbumin is specific for acute tryptophan loading, whereas gelatine is only partially effective for acute tryptophan depletion. Tryptophan 73-83 lactalbumin alpha Homo sapiens 33-50 25310453-6 2014 Among the binding residues, the C-terminal residues like aspartate (D) 116, glutamine (Q) 117, tryptophan (W) 118 and leucine (L) 119 are destabilized and disordered and can dock beta4GalT onto Ca(2+)-aLA. Tryptophan 95-105 lactalbumin alpha Homo sapiens 201-204