메뉴 건너뛰기




Volumn 61, Issue 28, 2013, Pages 6971-6981

Comprehensive analysis of nonenzymatic post-translational β-lactoglobulin modifications in processed milk by ultrahigh-performance liquid chromatography-tandem mass spectrometry

Author keywords

lactoglobulin; glycation; mass spectrometry; oxidation; processed milk; protein modification

Indexed keywords

GLYCATION; LACTOGLOBULIN; LIQUID CHROMATOGRAPHY-TANDEM MASS SPECTROMETRY; MULTIPLE REACTION MONITORING; PROCESSED MILK; PROTEIN MODIFICATIONS; SYSTEMATIC IDENTIFICATION; TANDEM MASS SPECTROMETRY;

EID: 84880379712     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf401549j     Document Type: Article
Times cited : (50)

References (50)
  • 2
    • 58849112552 scopus 로고    scopus 로고
    • Studies on the impact of glycation on the denaturation of whey proteins
    • Mulsow, B. B.; Jacob, M.; Henle, T. Studies on the impact of glycation on the denaturation of whey proteins Eur. Food Res. Technol. 2009, 228, 643-649
    • (2009) Eur. Food Res. Technol. , vol.228 , pp. 643-649
    • Mulsow, B.B.1    Jacob, M.2    Henle, T.3
  • 3
    • 78650117871 scopus 로고    scopus 로고
    • Protein damage in diabetes and uremia - Identifying hotspots of proteome damage where minimal modification is amplified to marked pathophysiological effect
    • Thornalley, P. J.; Rabbani, N. Protein damage in diabetes and uremia-Identifying hotspots of proteome damage where minimal modification is amplified to marked pathophysiological effect Free Radical Res. 2011, 45, 89-100
    • (2011) Free Radical Res. , vol.45 , pp. 89-100
    • Thornalley, P.J.1    Rabbani, N.2
  • 4
    • 47849096112 scopus 로고    scopus 로고
    • Identification and site-specific relative quantification of beta-lactoglobulin modifications in heated milk and dairy products
    • Meltretter, J.; Becker, C. M.; Pischetsrieder, M. Identification and site-specific relative quantification of beta-lactoglobulin modifications in heated milk and dairy products J. Agric. Food Chem. 2008, 56, 5165-5171
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 5165-5171
    • Meltretter, J.1    Becker, C.M.2    Pischetsrieder, M.3
  • 5
    • 77949837372 scopus 로고    scopus 로고
    • Identification of cysteine, methionine and tryptophan residues of actin oxidized in vivo during oxidative stress
    • Fedorova, M.; Kuleva, N.; Hoffmann, R. Identification of cysteine, methionine and tryptophan residues of actin oxidized in vivo during oxidative stress J. Proteome Res. 2010, 9, 1598-1609
    • (2010) J. Proteome Res. , vol.9 , pp. 1598-1609
    • Fedorova, M.1    Kuleva, N.2    Hoffmann, R.3
  • 6
    • 79959987571 scopus 로고    scopus 로고
    • Comprehensive identification of glycated peptides and their glycation motifs in plasma and erythrocytes of control and diabetic subjects
    • Zhang, Q.; Monroe, M. E.; Schepmoes, A. A.; Clauss, T. R.; Gritsenko, M. A.; Meng, D.; Petyuk, V. A.; Smith, R. D.; Metz, T. O. Comprehensive identification of glycated peptides and their glycation motifs in plasma and erythrocytes of control and diabetic subjects J. Proteome Res. 2011, 10, 3076-3088
    • (2011) J. Proteome Res. , vol.10 , pp. 3076-3088
    • Zhang, Q.1    Monroe, M.E.2    Schepmoes, A.A.3    Clauss, T.R.4    Gritsenko, M.A.5    Meng, D.6    Petyuk, V.A.7    Smith, R.D.8    Metz, T.O.9
  • 7
    • 0037081029 scopus 로고    scopus 로고
    • Artifact-free quantification of free 3-chlorotyrosine, 3-bromotyrosine, and 3-nitrotyrosine in human plasma by electron capture-negative chemical ionization gas chromatography mass spectrometry and liquid chromatography- electrospray ionization tandem mass spectrometry
    • Gaut, J. P.; Byun, J.; Tran, H. D.; Heinecke, J. W. Artifact-free quantification of free 3-chlorotyrosine, 3-bromotyrosine, and 3-nitrotyrosine in human plasma by electron capture-negative chemical ionization gas chromatography mass spectrometry and liquid chromatography-electrospray ionization tandem mass spectrometry Anal. Biochem. 2002, 300, 252-259
    • (2002) Anal. Biochem. , vol.300 , pp. 252-259
    • Gaut, J.P.1    Byun, J.2    Tran, H.D.3    Heinecke, J.W.4
  • 8
    • 34547753123 scopus 로고    scopus 로고
    • Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose
    • Meltretter, J.; Seeber, S.; Humeny, A.; Becker, C. M.; Pischetsrieder, M. Site-specific formation of Maillard, oxidation, and condensation products from whey proteins during reaction with lactose J. Agric. Food Chem. 2007, 55, 6096-6103
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 6096-6103
    • Meltretter, J.1    Seeber, S.2    Humeny, A.3    Becker, C.M.4    Pischetsrieder, M.5
  • 9
    • 84861136821 scopus 로고    scopus 로고
    • Comprehensive identification of novel post-translational modifications in cellular peroxiredoxin 6
    • Jeong, J.; Kim, Y.; Kyung Seong, J.; Lee, K. J. Comprehensive identification of novel post-translational modifications in cellular peroxiredoxin 6 Proteomics 2012, 12, 1452-1462
    • (2012) Proteomics , vol.12 , pp. 1452-1462
    • Jeong, J.1    Kim, Y.2    Kyung Seong, J.3    Lee, K.J.4
  • 10
    • 84862316500 scopus 로고    scopus 로고
    • Glycation products in infant formulas: Chemical, analytical and physiological aspects
    • Pischetsrieder, M.; Henle, T. Glycation products in infant formulas: Chemical, analytical and physiological aspects Amino Acids 2012, 42, 1111-1118
    • (2012) Amino Acids , vol.42 , pp. 1111-1118
    • Pischetsrieder, M.1    Henle, T.2
  • 11
    • 43449125934 scopus 로고    scopus 로고
    • Comparative LC-MS/MS profiling of free and protein-bound early and advanced glycation-induced lysine modifications in dairy products
    • Hegele, J.; Buetler, T.; Delatour, T. Comparative LC-MS/MS profiling of free and protein-bound early and advanced glycation-induced lysine modifications in dairy products Anal. Chim. Acta 2008, 617, 85-96
    • (2008) Anal. Chim. Acta , vol.617 , pp. 85-96
    • Hegele, J.1    Buetler, T.2    Delatour, T.3
  • 12
    • 34250785181 scopus 로고    scopus 로고
    • Direct determination of methionine sulfoxide in milk proteins by enzyme hydrolysis/high-performance liquid chromatography
    • Baxter, J. H.; Lai, C. S.; Phillips, R. R.; Dowlati, L.; Chio, J. J.; Luebbers, S. T.; Dimler, S. R.; Johns, P. W. Direct determination of methionine sulfoxide in milk proteins by enzyme hydrolysis/high-performance liquid chromatography J. Chromatogr. A 2007, 1157, 10-16
    • (2007) J. Chromatogr. A , vol.1157 , pp. 10-16
    • Baxter, J.H.1    Lai, C.S.2    Phillips, R.R.3    Dowlati, L.4    Chio, J.J.5    Luebbers, S.T.6    Dimler, S.R.7    Johns, P.W.8
  • 13
    • 67349112777 scopus 로고    scopus 로고
    • Quantitation of lysinoalanine in dairy products by liquid chromatography-mass spectrometry with selective ion monitoring
    • Calabrese, M. G.; Mamone, G.; Caira, S.; Ferranti, P.; Addeo, F. Quantitation of lysinoalanine in dairy products by liquid chromatography-mass spectrometry with selective ion monitoring Food Chem. 2009, 116, 799-805
    • (2009) Food Chem. , vol.116 , pp. 799-805
    • Calabrese, M.G.1    Mamone, G.2    Caira, S.3    Ferranti, P.4    Addeo, F.5
  • 14
    • 70449412192 scopus 로고    scopus 로고
    • Determination of furosine in thermally processed foods by hydrophilic interaction liquid chromatography
    • Gokmen, V.; Serpen, A.; Morales, F. J. Determination of furosine in thermally processed foods by hydrophilic interaction liquid chromatography J. AOAC Int. 2009, 92, 1460-1463
    • (2009) J. AOAC Int. , vol.92 , pp. 1460-1463
    • Gokmen, V.1    Serpen, A.2    Morales, F.J.3
  • 15
    • 79251526538 scopus 로고    scopus 로고
    • Mapping the glycoxidation product N(epsilon)-carboxymethyllysine in the milk proteome
    • Meyer, B.; Al-Diab, D.; Vollmer, G.; Pischetsrieder, M. Mapping the glycoxidation product N(epsilon)-carboxymethyllysine in the milk proteome Proteomics 2011, 11, 420-428
    • (2011) Proteomics , vol.11 , pp. 420-428
    • Meyer, B.1    Al-Diab, D.2    Vollmer, G.3    Pischetsrieder, M.4
  • 16
    • 84864359686 scopus 로고    scopus 로고
    • Distribution of protein oxidation products in the proteome of thermally processed milk
    • Meyer, B.; Baum, F.; Vollmer, G.; Pischetsrieder, M. Distribution of protein oxidation products in the proteome of thermally processed milk J. Agric. Food Chem. 2012, 60, 7306-7311
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 7306-7311
    • Meyer, B.1    Baum, F.2    Vollmer, G.3    Pischetsrieder, M.4
  • 17
    • 83655172685 scopus 로고    scopus 로고
    • Multistep ultrahigh performance liquid chromatography/tandem mass spectrometry analysis for untargeted quantification of glycating activity and identification of most relevant glycation products
    • Mittelmaier, S.; Pischetsrieder, M. Multistep ultrahigh performance liquid chromatography/tandem mass spectrometry analysis for untargeted quantification of glycating activity and identification of most relevant glycation products Anal. Chem. 2011, 83, 9660-9668
    • (2011) Anal. Chem. , vol.83 , pp. 9660-9668
    • Mittelmaier, S.1    Pischetsrieder, M.2
  • 19
    • 0037181327 scopus 로고    scopus 로고
    • Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry peptide mapping
    • Humeny, A.; Kislinger, T.; Becker, C. M.; Pischetsrieder, M. Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry peptide mapping J. Agric. Food Chem. 2002, 50, 2153-2160
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 2153-2160
    • Humeny, A.1    Kislinger, T.2    Becker, C.M.3    Pischetsrieder, M.4
  • 21
    • 22444446782 scopus 로고    scopus 로고
    • Assay of advanced glycation endproducts in selected beverages and food by liquid chromatography with tandem mass spectrometric detection
    • Ahmed, N.; Mirshekar-Syahkal, B.; Kennish, L.; Karachalias, N.; Babaei-Jadidi, R.; Thornalley, P. J. Assay of advanced glycation endproducts in selected beverages and food by liquid chromatography with tandem mass spectrometric detection Mol. Nutr. Food Res. 2005, 49, 691-699
    • (2005) Mol. Nutr. Food Res. , vol.49 , pp. 691-699
    • Ahmed, N.1    Mirshekar-Syahkal, B.2    Kennish, L.3    Karachalias, N.4    Babaei-Jadidi, R.5    Thornalley, P.J.6
  • 22
    • 79952177484 scopus 로고    scopus 로고
    • Proteomic analysis of temperature-dependent changes in stored UHT milk
    • Holland, J. W.; Gupta, R.; Deeth, H. C.; Alewood, P. F. Proteomic analysis of temperature-dependent changes in stored UHT milk J. Agric. Food Chem. 2011, 59, 1837-1846
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 1837-1846
    • Holland, J.W.1    Gupta, R.2    Deeth, H.C.3    Alewood, P.F.4
  • 23
    • 0035835401 scopus 로고    scopus 로고
    • New high-performance liquid chromatographic method for the detection of picolinic acid in biological fluids
    • Dazzi, C.; Candiano, G.; Massazza, S.; Ponzetto, A.; Varesio, L. New high-performance liquid chromatographic method for the detection of picolinic acid in biological fluids J. Chromatogr. B Biomed. Sci. Appl. 2001, 751, 61-68
    • (2001) J. Chromatogr. B Biomed. Sci. Appl. , vol.751 , pp. 61-68
    • Dazzi, C.1    Candiano, G.2    Massazza, S.3    Ponzetto, A.4    Varesio, L.5
  • 24
    • 0032143427 scopus 로고    scopus 로고
    • Effect of heating on Maillard reactions in milk
    • van Boekel, M. A. J. S. Effect of heating on Maillard reactions in milk Food Chem. 1998, 62, 403-414
    • (1998) Food Chem. , vol.62 , pp. 403-414
    • Van Boekel, M.A.J.S.1
  • 25
    • 0022931516 scopus 로고
    • Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
    • Ahmed, M. U.; Thorpe, S. R.; Baynes, J. W. Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein J. Biol. Chem. 1986, 261, 4889-4894
    • (1986) J. Biol. Chem. , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 26
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction
    • Glomb, M. A.; Monnier, V. M. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction J. Biol. Chem. 1995, 270, 10017-10026
    • (1995) J. Biol. Chem. , vol.270 , pp. 10017-10026
    • Glomb, M.A.1    Monnier, V.M.2
  • 27
    • 2542509987 scopus 로고    scopus 로고
    • Formation of amino acids by reaction of glucose and xylose with primary amines
    • Buettner, U.; Ochs, S.; Severin, T. Formation of amino acids by reaction of glucose and xylose with primary amines Carbohydr. Res. 1996, 291, 175-181
    • (1996) Carbohydr. Res. , vol.291 , pp. 175-181
    • Buettner, U.1    Ochs, S.2    Severin, T.3
  • 28
    • 34247844598 scopus 로고    scopus 로고
    • Studies on N-terminal glycation of peptides in hypoallergenic infant formulas: Quantification of α- N -(2-furoylmethyl) amino acids
    • Penndorf, I.; Biedermann, D.; Maurer, S. V.; Henle, T. Studies on N-terminal glycation of peptides in hypoallergenic infant formulas: Quantification of α- N -(2-furoylmethyl) amino acids J. Agric. Food Chem. 2007, 55, 723-727
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 723-727
    • Penndorf, I.1    Biedermann, D.2    Maurer, S.V.3    Henle, T.4
  • 29
    • 78650250717 scopus 로고    scopus 로고
    • Comparison of modification sites formed on human serum albumin at various stages of glycation
    • Barnaby, O. S.; Cerny, R. L.; Clarke, W.; Hage, D. S. Comparison of modification sites formed on human serum albumin at various stages of glycation Clin. Chim. Acta 2011, 412, 277-285
    • (2011) Clin. Chim. Acta , vol.412 , pp. 277-285
    • Barnaby, O.S.1    Cerny, R.L.2    Clarke, W.3    Hage, D.S.4
  • 30
    • 0032492551 scopus 로고    scopus 로고
    • The generation of superoxide anions in glycation reactions with sugars, osones, and 3-deoxyosones
    • Ortwerth, B. J.; James, H.; Simpson, G.; Linetsky, M. The generation of superoxide anions in glycation reactions with sugars, osones, and 3-deoxyosones Biochem. Biophys. Res. Commun. 1998, 245, 161-165
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 161-165
    • Ortwerth, B.J.1    James, H.2    Simpson, G.3    Linetsky, M.4
  • 31
    • 0036441178 scopus 로고    scopus 로고
    • Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction
    • Akagawa, M.; Sasaki, T.; Suyama, K. Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction Eur. J. Biochem. 2002, 269, 5451-5458
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5451-5458
    • Akagawa, M.1    Sasaki, T.2    Suyama, K.3
  • 32
    • 78049270042 scopus 로고    scopus 로고
    • 3-deoxygalactosone, a "new" 1,2-dicarbonyl compound in milk products
    • Hellwig, M.; Degen, J.; Henle, T. 3-deoxygalactosone, a "new" 1,2-dicarbonyl compound in milk products J. Agric. Food Chem. 2010, 58, 10752-10760
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 10752-10760
    • Hellwig, M.1    Degen, J.2    Henle, T.3
  • 33
    • 33846595607 scopus 로고    scopus 로고
    • Detection and identification of arginine modifications on methylglyoxal-modified ribonuclease by mass spectrometric analysis
    • Brock, J. W.; Cotham, W. E.; Thorpe, S. R.; Baynes, J. W.; Ames, J. M. Detection and identification of arginine modifications on methylglyoxal-modified ribonuclease by mass spectrometric analysis J. Mass Spectrom. 2007, 42, 89-100
    • (2007) J. Mass Spectrom. , vol.42 , pp. 89-100
    • Brock, J.W.1    Cotham, W.E.2    Thorpe, S.R.3    Baynes, J.W.4    Ames, J.M.5
  • 35
    • 0000611410 scopus 로고
    • Degradation of lactose during heating of milk. 1. Reaction pathways
    • Berg, H. E.; van Boekel, M. A. J. S. Degradation of lactose during heating of milk. 1. Reaction pathways Neth. Milk Dairy J. 1994, 48, 157-175
    • (1994) Neth. Milk Dairy J. , vol.48 , pp. 157-175
    • Berg, H.E.1    Van Boekel, M.A.J.S.2
  • 36
    • 33745779635 scopus 로고    scopus 로고
    • Non-enzymatic model glycation reactions - A comprehensive study of the reactivity of a modified arginine with aldehydic and diketonic dicarbonyl compounds by electrospray mass spectrometry
    • Saraiva, M. A.; Borges, C. M.; Florencio, M. H. Non-enzymatic model glycation reactions-A comprehensive study of the reactivity of a modified arginine with aldehydic and diketonic dicarbonyl compounds by electrospray mass spectrometry J. Mass Spectrom. 2006, 41, 755-770
    • (2006) J. Mass Spectrom. , vol.41 , pp. 755-770
    • Saraiva, M.A.1    Borges, C.M.2    Florencio, M.H.3
  • 37
    • 1142299461 scopus 로고    scopus 로고
    • Solid-state glycation of beta-lactoglobulin by lactose and galactose: Localization of the modified amino acids using mass spectrometric techniques
    • Fenaille, F.; Morgan, F.; Parisod, V.; Tabet, J. C.; Guy, P. A. Solid-state glycation of beta-lactoglobulin by lactose and galactose: Localization of the modified amino acids using mass spectrometric techniques J. Mass Spectrom. 2004, 39, 16-28
    • (2004) J. Mass Spectrom. , vol.39 , pp. 16-28
    • Fenaille, F.1    Morgan, F.2    Parisod, V.3    Tabet, J.C.4    Guy, P.A.5
  • 38
    • 12844260763 scopus 로고    scopus 로고
    • Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease
    • Schoneich, C. Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease Biochim. Biophys. Acta 2005, 1703, 111-119
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 111-119
    • Schoneich, C.1
  • 40
    • 0000217491 scopus 로고    scopus 로고
    • Oxidation of free tryptophan and tryptophan residues in peptides and proteins
    • Simat, T. J.; Steinhart, H. Oxidation of free tryptophan and tryptophan residues in peptides and proteins J. Agric. Food Chem. 1998, 46, 490-498
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 490-498
    • Simat, T.J.1    Steinhart, H.2
  • 41
    • 0030996762 scopus 로고    scopus 로고
    • Effect of iron and lactose supplementation of milk on the Maillard reaction and tryptophan content
    • Birlouez-Aragon, I.; Moreaux, V.; Nicolas, M.; Ducauze, C. J. Effect of iron and lactose supplementation of milk on the Maillard reaction and tryptophan content Food Addit. Contam. 1997, 14, 381-388
    • (1997) Food Addit. Contam. , vol.14 , pp. 381-388
    • Birlouez-Aragon, I.1    Moreaux, V.2    Nicolas, M.3    Ducauze, C.J.4
  • 42
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies, K. J.; Delsignore, M. E.; Lin, S. W. Protein damage and degradation by oxygen radicals. II. Modification of amino acids J. Biol. Chem. 1987, 262, 9902-9907
    • (1987) J. Biol. Chem. , vol.262 , pp. 9902-9907
    • Davies, K.J.1    Delsignore, M.E.2    Lin, S.W.3
  • 43
    • 0017786428 scopus 로고
    • Formation of dehydroalanine, lanthionine and lysinoalanine during heat treatment of beta-lactoglobuline A
    • Watanabe, K.; Klostermeyer, H. Formation of dehydroalanine, lanthionine and lysinoalanine during heat treatment of beta-lactoglobuline A Z. Lebensm. Unters. Forsch. 1977, 164, 77-79
    • (1977) Z. Lebensm. Unters. Forsch. , vol.164 , pp. 77-79
    • Watanabe, K.1    Klostermeyer, H.2
  • 45
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • Tyler-Cross, R.; Schirch, V. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides J. Biol. Chem. 1991, 266, 22549-22556
    • (1991) J. Biol. Chem. , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 46
    • 0031922415 scopus 로고    scopus 로고
    • On the kinetics of heat-induced deamidation and breakdown of caseinate
    • Metwalli, A. A. M.; van Boekel, M. A. J. S. On the kinetics of heat-induced deamidation and breakdown of caseinate Food Chem. 1998, 61, 53-61
    • (1998) Food Chem. , vol.61 , pp. 53-61
    • Metwalli, A.A.M.1    Van Boekel, M.A.J.S.2
  • 47
    • 0017339161 scopus 로고
    • Availability of the true Schiff's bases of lysine. Chemical evaluation of the Schiff's base between lysine and lactose in milk
    • Finot, P. A.; Bujard, E.; Mottu, F.; Mauron, J. Availability of the true Schiff's bases of lysine. Chemical evaluation of the Schiff's base between lysine and lactose in milk Adv. Exp. Med. Biol. 1977, 86B, 343-365
    • (1977) Adv. Exp. Med. Biol. , vol.86 , pp. 343-365
    • Finot, P.A.1    Bujard, E.2    Mottu, F.3    Mauron, J.4
  • 49
    • 84895901773 scopus 로고    scopus 로고
    • N -ε-fructosyllysine and N -ε-carboxymethyllysine, but not lysinoalanine, are available for absorption after simulated gastrointestinal digestion
    • 10.1007/s00726-013-1501-5
    • Hellwig, M.; Matthes, R.; Peto, A.; Lobner, J.; Henle, T. N -ε-fructosyllysine and N -ε-carboxymethyllysine, but not lysinoalanine, are available for absorption after simulated gastrointestinal digestion Amino Acids 2013, 10.1007/s00726-013-1501-5
    • (2013) Amino Acids
    • Hellwig, M.1    Matthes, R.2    Peto, A.3    Lobner, J.4    Henle, T.5
  • 50
    • 34447560057 scopus 로고    scopus 로고
    • Mutational analysis of immunoglobulin E-binding epitopes of beta-casein and beta-lactoglobulin showed a heterogeneous pattern of critical amino acids between individual patients and pooled sera
    • Cocco, R. R.; Jarvinen, K. M.; Han, N.; Beyer, K.; Sampson, H. A. Mutational analysis of immunoglobulin E-binding epitopes of beta-casein and beta-lactoglobulin showed a heterogeneous pattern of critical amino acids between individual patients and pooled sera Clin. Exp. Allergy 2007, 37, 831-838-838
    • (2007) Clin. Exp. Allergy , vol.37 , pp. 831
    • Cocco, R.R.1    Jarvinen, K.M.2    Han, N.3    Beyer, K.4    Sampson, H.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.