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Volumn 18, Issue 4, 2017, Pages

Studying lactoferrin N-glycosylation

Author keywords

Bioinfomatic libraries; Deglycosylating enzymes; Lactoferrin; Mass spectrophotometry; N glycans; Structure activity studies

Indexed keywords

LACTOFERRIN; GLYCOPROTEIN; ISOPROTEIN; MILK PROTEIN; POLYSACCHARIDE;

EID: 85018525914     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms18040870     Document Type: Review
Times cited : (120)

References (70)
  • 2
    • 0001618922 scopus 로고
    • Isolation of an iron-containing red protein from human milk
    • [CrossRef]
    • Johanson, B. Isolation of an iron-containing red protein from human milk. Acta Chem. Scand. 1960, 14, 510-512. [CrossRef]
    • (1960) Acta Chem. Scand , vol.14 , pp. 510-512
    • Johanson, B.1
  • 3
    • 0027467647 scopus 로고
    • Lactoferrin, lactoferrin receptors and iron metabolism
    • [PubMed]
    • Iyer, S.; Lonnerdal, B. Lactoferrin, lactoferrin receptors and iron metabolism. Eur. J. Clin. Nutr. 1993, 47, 232-241. [PubMed]
    • (1993) Eur. J. Clin. Nutr , vol.47 , pp. 232-241
    • Iyer, S.1    Lonnerdal, B.2
  • 4
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • [PubMed]
    • Levay, P.F.; Viljoen, M. Lactoferrin: A general review. Haematologica 1995, 80, 252-267. [PubMed]
    • (1995) Haematologica , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 5
    • 0009815581 scopus 로고    scopus 로고
    • Milk ingredients as nutraceuticals
    • [CrossRef]
    • Steijns, J.M. Milk ingredients as nutraceuticals. Int. J. Dairy Technol. 2001, 54, 81-88. [CrossRef]
    • (2001) Int. J. Dairy Technol , vol.54 , pp. 81-88
    • Steijns, J.M.1
  • 6
    • 0025615473 scopus 로고
    • Concentrations of lactoferrin and iron in human milk at different stages of lactation
    • [CrossRef] [PubMed]
    • Hirai, Y.; Kawakata, N.; Satoh, K.; Ikeda, Y.; Hisayasu, S.; Orimo, H.; Yoshino, Y. Concentrations of lactoferrin and iron in human milk at different stages of lactation. J. Nutr. Sci. Vitaminol. 1990, 36, 531. [CrossRef] [PubMed]
    • (1990) J. Nutr. Sci. Vitaminol , vol.36 , pp. 531
    • Hirai, Y.1    Kawakata, N.2    Satoh, K.3    Ikeda, Y.4    Hisayasu, S.5    Orimo, H.6    Yoshino, Y.7
  • 9
    • 0026293901 scopus 로고
    • Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin
    • [CrossRef]
    • Tomita, M.; Bellamy, W.; Takase, M.; Yamauchi, K.; Wakabayashi, H.; Kawase, K. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J. Dairy Sci. 1991, 74, 4137-4142. [CrossRef]
    • (1991) J. Dairy Sci , vol.74 , pp. 4137-4142
    • Tomita, M.1    Bellamy, W.2    Takase, M.3    Yamauchi, K.4    Wakabayashi, H.5    Kawase, K.6
  • 10
    • 3342947834 scopus 로고    scopus 로고
    • Protection against infections by oral lactoferrin: Evaluation in animal models
    • [CrossRef] [PubMed]
    • Teraguchi, S.; Wakabayashi, H.; Kuwata, H.; Yamauchi, K.; Tamura, Y. Protection against infections by oral lactoferrin: Evaluation in animal models. Biometals 2004, 17, 231-234. [CrossRef] [PubMed]
    • (2004) Biometals , vol.17 , pp. 231-234
    • Teraguchi, S.1    Wakabayashi, H.2    Kuwata, H.3    Yamauchi, K.4    Tamura, Y.5
  • 11
    • 20444401969 scopus 로고    scopus 로고
    • Pepsin-digested bovine lactoferrin induces apoptotic cell death with JNK/SAPK activation in oral cancer cells
    • [CrossRef] [PubMed]
    • Sakai, T.; Banno, Y.; Kato, Y.; Nozawa, Y.; Kawaguchi, M. Pepsin-digested bovine lactoferrin induces apoptotic cell death with JNK/SAPK activation in oral cancer cells. J. Pharmacol. Sci. 2005, 98, 41-48. [CrossRef] [PubMed]
    • (2005) J. Pharmacol. Sci , vol.98 , pp. 41-48
    • Sakai, T.1    Banno, Y.2    Kato, Y.3    Nozawa, Y.4    Kawaguchi, M.5
  • 12
    • 19944419885 scopus 로고    scopus 로고
    • Expression profile of immune response genes in patients with severe acute respiratory syndrome
    • [CrossRef] [PubMed]
    • Reghunathan, R.; Jayapal, M.; Hsu, L.-Y.; Chng, H.-H.; Tai, D.; Leung, B.P.; Melendez, A.J. Expression profile of immune response genes in patients with severe acute respiratory syndrome. BMC Immunol. 2005, 6, 1. [CrossRef] [PubMed]
    • (2005) BMC Immunol , vol.1 , pp. 6
    • Reghunathan, R.1    Jayapal, M.2    Hsu, L.-Y.3    Chng, H.-H.4    Tai, D.5    Leung, B.P.6    Melendez, A.J.7
  • 13
    • 0037051529 scopus 로고    scopus 로고
    • Effects of natural phenolic compounds on the antioxidant activity of lactoferrin in liposomes and oil-in-water emulsions
    • [CrossRef] [PubMed]
    • Medina, I.; Tombo, I.; Satué-Gracia, M.T.; German, J.B.; Frankel, E.N. Effects of natural phenolic compounds on the antioxidant activity of lactoferrin in liposomes and oil-in-water emulsions. J. Agric. Food Chem. 2002, 50, 2392-2399. [CrossRef] [PubMed]
    • (2002) J. Agric. Food Chem , vol.50 , pp. 2392-2399
    • Medina, I.1    Tombo, I.2    Satué-Gracia, M.T.3    German, J.B.4    Frankel, E.N.5
  • 15
    • 0035751230 scopus 로고    scopus 로고
    • Characterization of glycans in a lactoferrin isoform, lactoferrin-a
    • [CrossRef]
    • Wei, Z.; Nishimura, T.; Yoshida, S. Characterization of glycans in a lactoferrin isoform, lactoferrin-a. J. Dairy Sci. 2001, 84, 2584-2590. [CrossRef]
    • (2001) J. Dairy Sci , vol.84 , pp. 2584-2590
    • Wei, Z.1    Nishimura, T.2    Yoshida, S.3
  • 16
    • 84888416425 scopus 로고    scopus 로고
    • Human milk secretory immunoglobulin a and lactoferrin N-glycans are altered in women with gestational diabetes mellitus
    • [CrossRef] [PubMed]
    • Smilowitz, J.T.; Totten, S.M.; Huang, J.; Grapov, D.; Durham, H.A.; Lammi-Keefe, C.J.; Lebrilla, C.; German, J.B. Human milk secretory immunoglobulin a and lactoferrin N-glycans are altered in women with gestational diabetes mellitus. J. Nutr. 2013, 143, 1906-1912. [CrossRef] [PubMed]
    • (2013) J. Nutr , vol.143 , pp. 1906-1912
    • Smilowitz, J.T.1    Totten, S.M.2    Huang, J.3    Grapov, D.4    Durham, H.A.5    Lammi-Keefe, C.J.6    Lebrilla, C.7    German, J.B.8
  • 17
    • 77957017407 scopus 로고    scopus 로고
    • Analyses of diverse mammals’ milk and lactoferrin glycans using five pathogenic bacterial lectins
    • [CrossRef]
    • Zinger-Yosovich, K.D.; Sudakevitz, D.; Iluz, D.; Gilboa-Garber, N. Analyses of diverse mammals’ milk and lactoferrin glycans using five pathogenic bacterial lectins. Food Chem. 2011, 124, 1335-1342. [CrossRef]
    • (2011) Food Chem , vol.124 , pp. 1335-1342
    • Zinger-Yosovich, K.D.1    Sudakevitz, D.2    Iluz, D.3    Gilboa-Garber, N.4
  • 18
    • 0028630582 scopus 로고
    • Primary and three-dimensional structure of lactotransferrin (Lactoferrin) glycans
    • Springer: Berlin, Germany
    • Spik, G.; Coddeville, B.; Mazurier, J.; Bourne, Y.; Cambillaut, C.; Montreuil, J. Primary and three-dimensional structure of lactotransferrin (lactoferrin) glycans. In Lactoferrin; Springer: Berlin, Germany, 1994; pp. 21-32.
    • (1994) In Lactoferrin , pp. 21-32
    • Spik, G.1    Coddeville, B.2    Mazurier, J.3    Bourne, Y.4    Cambillaut, C.5    Montreuil, J.6
  • 19
    • 23744501922 scopus 로고    scopus 로고
    • The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin
    • [CrossRef] [PubMed]
    • Thomassen, E.A.; van Veen, H.A.; van Berkel, P.H.; Nuijens, J.H.; Abrahams, J.P. The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin. Transgenic Res. 2005, 14, 397-405. [CrossRef] [PubMed]
    • (2005) Transgenic Res , vol.14 , pp. 397-405
    • Thomassen, E.A.1    van Veen, H.A.2    van Berkel, P.H.3    Nuijens, J.H.4    Abrahams, J.P.5
  • 20
    • 84879838324 scopus 로고    scopus 로고
    • Expression of recombinant human lactoferrin in transgenic alfalfa plants
    • [CrossRef]
    • Stefanova, G.; Slavov, S.; Gecheff, K.; Vlahova, M.; Atanassov, A. Expression of recombinant human lactoferrin in transgenic alfalfa plants. Biol. Plant. 2013, 57, 457-464. [CrossRef]
    • (2013) Biol. Plant , vol.57 , pp. 457-464
    • Stefanova, G.1    Slavov, S.2    Gecheff, K.3    Vlahova, M.4    Atanassov, A.5
  • 21
    • 0036503143 scopus 로고    scopus 로고
    • Activated lactoferrin—A new approach to meat safety
    • Naidu, A. Activated lactoferrin—A new approach to meat safety. Food Technol. 2002, 56, 40-45.
    • (2002) Food Technol , vol.56 , pp. 40-45
    • Naidu, A.1
  • 24
    • 0015219737 scopus 로고
    • Molecular weight, single-chain structure and amino acid composition of human lactoferrin
    • [CrossRef] [PubMed]
    • Querinjean, P.; Masson, P.L.; Heremans, J.F. Molecular weight, single-chain structure and amino acid composition of human lactoferrin. Eur. J. Biochem. 1971, 20, 420-425. [CrossRef] [PubMed]
    • (1971) Eur. J. Biochem , vol.20 , pp. 420-425
    • Querinjean, P.1    Masson, P.L.2    Heremans, J.F.3
  • 25
    • 0016284941 scopus 로고
    • Amino acid sequence of cysteic peptides of lactoferrin and demonstration of similarities between lactoferrin and transferrin. Biochim. Biophys
    • [CrossRef]
    • Bluard-Deconinck, J.-M.; Masson, P.L.; Osinski, P.A.; Heremans, J.F. Amino acid sequence of cysteic peptides of lactoferrin and demonstration of similarities between lactoferrin and transferrin. Biochim. Biophys. Acta BBA Protein Struct. 1974, 365, 311-317. [CrossRef]
    • (1974) Acta BBA Protein Struct , vol.365 , pp. 311-317
    • Bluard-Deconinck, J.-M.1    Masson, P.L.2    Osinski, P.A.3    Heremans, J.F.4
  • 26
    • 0024393966 scopus 로고
    • Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity
    • [CrossRef] [PubMed]
    • Furmanski, P.; Li, Z.; Fortuna, M.B.; Swamy, C.; Das, M.R. Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity. J. Exp. Med. 1989, 170, 415-429. [CrossRef] [PubMed]
    • (1989) J. Exp. Med , vol.170 , pp. 415-429
    • Furmanski, P.1    Li, Z.2    Fortuna, M.B.3    Swamy, C.4    Das, M.R.5
  • 27
    • 0000154631 scopus 로고
    • Structure and reactivity of transferrins
    • Baker, E. Structure and reactivity of transferrins. Adv. Inorg. Chem. 1994, 41, 389-463.
    • (1994) Adv. Inorg. Chem , vol.41 , pp. 389-463
    • Baker, E.1
  • 28
    • 0017148443 scopus 로고
    • The effect of trypsin on bovine transferrin and lactoferrin. Biochim. Biophys
    • [CrossRef]
    • Brock, J.; Arzabe, F.; Lampreave, F.; Pineiro, A. The effect of trypsin on bovine transferrin and lactoferrin. Biochim. Biophys. Acta BBA Protein Struct. 1976, 446, 214-225. [CrossRef]
    • (1976) Acta BBA Protein Struct , vol.446 , pp. 214-225
    • Brock, J.1    Arzabe, F.2    Lampreave, F.3    Pineiro, A.4
  • 29
    • 0020508495 scopus 로고
    • The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrum: Unusual resistance of human apolactoferrin to proteolytic digestion
    • [CrossRef]
    • Brines, R.; Brock, J. The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrum: Unusual resistance of human apolactoferrin to proteolytic digestion. Biochim. Biophys. Acta BBA Gen. Subj. 1983, 759, 229-235. [CrossRef]
    • (1983) Biochim. Biophys. Acta BBA Gen. Subj , vol.759 , pp. 229-235
    • Brines, R.1    Brock, J.2
  • 30
    • 1342322699 scopus 로고    scopus 로고
    • The role of n-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis
    • [CrossRef] [PubMed]
    • Van Veen, H.A.; Geerts, M.E.; van Berkel, P.H.; Nuijens, J.H. The role of n-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis. Eur. J. Biochem. 2004, 271, 678-684. [CrossRef] [PubMed]
    • (2004) Eur. J. Biochem , vol.271 , pp. 678-684
    • van Veen, H.A.1    Geerts, M.E.2    van Berkel, P.H.3    Nuijens, J.H.4
  • 32
    • 0027650408 scopus 로고
    • Brock, J.H. Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes
    • [CrossRef] [PubMed]
    • Oria, R.; Ismail, M.; Sánchez, L.; Calvo, M.; Brock, J.H. Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes. J. Dairy Res. 1993, 60, 363-369. [CrossRef] [PubMed]
    • (1993) J. Dairy Res , vol.60 , pp. 363-369
    • Oria, R.1    Ismail, M.2    Sánchez, L.3    Calvo, M.4
  • 33
    • 34547691640 scopus 로고    scopus 로고
    • Effect of iron saturation on the recovery of lactoferrin in rennet whey coming from heat-treated skim milk
    • [CrossRef] [PubMed]
    • Brisson, G.; Britten, M.; Pouliot, Y. Effect of iron saturation on the recovery of lactoferrin in rennet whey coming from heat-treated skim milk. J. Dairy Sci. 2007, 90, 2655-2664. [CrossRef] [PubMed]
    • (2007) J. Dairy Sci , vol.90 , pp. 2655-2664
    • Brisson, G.1    Britten, M.2    Pouliot, Y.3
  • 34
    • 0032514621 scopus 로고    scopus 로고
    • Human milk lactoferrin inactivates two putative colonization factors expressed by haemophilus influenzae
    • [CrossRef] [PubMed]
    • Qiu, J.; Hendrixson, D.R.; Baker, E.N.; Murphy, T.F.; Geme, J.W.S.; Plaut, A.G. Human milk lactoferrin inactivates two putative colonization factors expressed by haemophilus influenzae. Proc. Natl. Acad. Sci. USA 1998, 95, 12641-12646. [CrossRef] [PubMed]
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12641-12646
    • Qiu, J.1    Hendrixson, D.R.2    Baker, E.N.3    Murphy, T.F.4    Geme, J.W.S.5    Plaut, A.G.6
  • 35
    • 33748416650 scopus 로고    scopus 로고
    • Interactions of lactoferrin with cells involved in immune function this paper is one of a selection of papers published in this special issue, entitled 7th international conference on lactoferrin: Structure, function, and applications, and has undergone the journal‘s usual peer review process
    • [PubMed]
    • Legrand, D.; Elass, E.; Carpentier, M.; Mazurier, J. Interactions of lactoferrin with cells involved in immune function this paper is one of a selection of papers published in this special issue, entitled 7th international conference on lactoferrin: Structure, function, and applications, and has undergone the journal‘s usual peer review process. Biochem. Cell Biol. 2006, 84, 282-290. [PubMed]
    • (2006) Biochem. Cell Biol , vol.84 , pp. 282-290
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 37
    • 0028231589 scopus 로고
    • Human lactoferrin inhibits growth of solid tumors and development of experimental metastases in mice
    • [PubMed]
    • Bezault, J.; Bhimani, R.; Wiprovnick, J.; Furmanski, P. Human lactoferrin inhibits growth of solid tumors and development of experimental metastases in mice. Cancer Res. 1994, 54, 2310-2312. [PubMed]
    • (1994) Cancer Res , vol.54 , pp. 2310-2312
    • Bezault, J.1    Bhimani, R.2    Wiprovnick, J.3    Furmanski, P.4
  • 38
    • 0015168183 scopus 로고
    • Inhibition of growth of candida albicans by iron-unsaturated lactoferrin: Relation to host-defense mechanisms in chronic mucocutaneous candidiasis
    • [CrossRef] [PubMed]
    • Kirkpatrick, C.H.; Green, I.; Rich, R.R.; Schade, A.L. Inhibition of growth of candida albicans by iron-unsaturated lactoferrin: Relation to host-defense mechanisms in chronic mucocutaneous candidiasis. J. Infect. Dis. 1971, 124, 539-544. [CrossRef] [PubMed]
    • (1971) J. Infect. Dis , vol.124 , pp. 539-544
    • Kirkpatrick, C.H.1    Green, I.2    Rich, R.R.3    Schade, A.L.4
  • 39
    • 3342897649 scopus 로고    scopus 로고
    • Neonatal small bowel epithelia: Enhancing anti-bacterial defense with lactoferrin and lactobacillus gg
    • [CrossRef] [PubMed]
    • Sherman, M.P.; Bennett, S.H.; Hwang, F.F.; Yu, C. Neonatal small bowel epithelia: Enhancing anti-bacterial defense with lactoferrin and lactobacillus gg. Biometals 2004, 17, 285-289. [CrossRef] [PubMed]
    • (2004) Biometals , vol.17 , pp. 285-289
    • Sherman, M.P.1    Bennett, S.H.2    Hwang, F.F.3    Yu, C.4
  • 40
    • 0032827980 scopus 로고    scopus 로고
    • Ability of lactoferrin to promote the growth of bifidobacterium spp. In vitro is independent of receptor binding capacity and iron saturation level
    • [CrossRef] [PubMed]
    • Petschow, B.; Talbott, R.; Batema, R. Ability of lactoferrin to promote the growth of bifidobacterium spp. In vitro is independent of receptor binding capacity and iron saturation level. J. Med. Microbiol. 1999, 48, 541-549. [CrossRef] [PubMed]
    • (1999) J. Med. Microbiol , vol.48 , pp. 541-549
    • Petschow, B.1    Talbott, R.2    Batema, R.3
  • 41
    • 84971472998 scopus 로고    scopus 로고
    • Oligosaccharides released from milk glycoproteins are selective growth substrates for infant-associated bifidobacteria
    • [CrossRef] [PubMed]
    • Karav, S.; Le Parc, A.; de Moura, J.M.L.N.; Frese, S.A.; Kirmiz, N.; Block, D.E.; Barile, D.; Mills, D.A. Oligosaccharides released from milk glycoproteins are selective growth substrates for infant-associated bifidobacteria. Appl. Environ. Microbiol. 2016, 82, 3622-3630. [CrossRef] [PubMed]
    • (2016) Appl. Environ. Microbiol , vol.82 , pp. 3622-3630
    • Karav, S.1    Le Parc, A.2    de Moura, J.M.L.N.3    Frese, S.A.4    Kirmiz, N.5    Block, D.E.6    Barile, D.7    Mills, D.A.8
  • 42
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • [CrossRef] [PubMed]
    • Brock, J.H. The physiology of lactoferrin. Biochem. Cell. Biol. 2002, 80, 1-6. [CrossRef] [PubMed]
    • (2002) Biochem. Cell. Biol , vol.80 , pp. 1-6
    • Brock, J.H.1
  • 44
    • 55149093179 scopus 로고    scopus 로고
    • Cattle mammary bioreactor generated by a novel procedure of transgenic cloning for large-scale production of functional human lactoferrin
    • [CrossRef] [PubMed]
    • Yang, P.; Wang, J.; Gong, G.; Sun, X.; Zhang, R.; Du, Z.; Liu, Y.; Li, R.; Ding, F.; Tang, B. Cattle mammary bioreactor generated by a novel procedure of transgenic cloning for large-scale production of functional human lactoferrin. PLoS ONE 2008, 3, e3453. [CrossRef] [PubMed]
    • (2008) Plos ONE , vol.3
    • Yang, P.1    Wang, J.2    Gong, G.3    Sun, X.4    Zhang, R.5    Du, Z.6    Liu, Y.7    Li, R.8    Ding, F.9    Tang, B.10
  • 45
    • 77957019333 scopus 로고    scopus 로고
    • Recombinant human lactoferrin: A valuable protein for pharmaceutical products and functional foods
    • [CrossRef] [PubMed]
    • Conesa, C.; Calvo, M.; Sánchez, L. Recombinant human lactoferrin: A valuable protein for pharmaceutical products and functional foods. Biotechnol. Adv. 2010, 28, 831-838. [CrossRef] [PubMed]
    • (2010) Biotechnol. Adv , vol.28 , pp. 831-838
    • Conesa, C.1    Calvo, M.2    Sánchez, L.3
  • 46
    • 79951996840 scopus 로고    scopus 로고
    • Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle
    • [CrossRef] [PubMed]
    • Yu, T.; Guo, C.; Wang, J.; Hao, P.; Sui, S.; Chen, X.; Zhang, R.; Wang, P.; Yu, G.; Zhang, L. Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle. Glycobiology 2011, 21, 206-224. [CrossRef] [PubMed]
    • (2011) Glycobiology , vol.21 , pp. 206-224
    • Yu, T.1    Guo, C.2    Wang, J.3    Hao, P.4    Sui, S.5    Chen, X.6    Zhang, R.7    Wang, P.8    Yu, G.9    Zhang, L.10
  • 47
    • 84938962772 scopus 로고    scopus 로고
    • Production of human lactoferrin and lysozyme in the milk of transgenic dairy animals: Past, present, and future
    • [CrossRef] [PubMed]
    • Cooper, C.A.; Maga, E.A.; Murray, J.D. Production of human lactoferrin and lysozyme in the milk of transgenic dairy animals: Past, present, and future. Transgenic Res. 2015, 24, 605-614. [CrossRef] [PubMed]
    • (2015) Transgenic Res , vol.24 , pp. 605-614
    • Cooper, C.A.1    Maga, E.A.2    Murray, J.D.3
  • 48
    • 84861416827 scopus 로고    scopus 로고
    • Transgenic milk containing recombinant human lactoferrin modulates the intestinal flora in piglets 1. This article is part of a special issue entitled lactoferrin and has undergone the journal’s usual peer review process
    • [CrossRef] [PubMed]
    • Hu, W.; Zhao, J.; Wang, J.; Yu, T.; Wang, J.; Li, N. Transgenic milk containing recombinant human lactoferrin modulates the intestinal flora in piglets 1. This article is part of a special issue entitled lactoferrin and has undergone the journal’s usual peer review process. Biochem. Cell Biol. 2012, 90, 485-496. [CrossRef] [PubMed]
    • (2012) Biochem. Cell Biol , vol.90 , pp. 485-496
    • Hu, W.1    Zhao, J.2    Wang, J.3    Yu, T.4    Wang, J.5
  • 49
    • 84869765075 scopus 로고    scopus 로고
    • Comprehensive assessment of milk composition in transgenic cloned cattle
    • [CrossRef] [PubMed]
    • Zhang, R.; Guo, C.; Sui, S.; Yu, T.; Wang, J.; Li, N. Comprehensive assessment of milk composition in transgenic cloned cattle. PLoS ONE 2012, 7, e49697. [CrossRef] [PubMed]
    • (2012) Plos ONE , vol.7
    • Zhang, R.1    Guo, C.2    Sui, S.3    Yu, T.4    Wang, J.5    Li, N.6
  • 50
    • 58149125767 scopus 로고    scopus 로고
    • A structural framework for understanding the multifunctional character of lactoferrin
    • [CrossRef] [PubMed]
    • Baker, E.N.; Baker, H.M. A structural framework for understanding the multifunctional character of lactoferrin. Biochimie 2009, 91, 3-10. [CrossRef] [PubMed]
    • (2009) Biochimie , vol.91 , pp. 3-10
    • Baker, E.N.1    Baker, H.M.2
  • 51
    • 0028813886 scopus 로고
    • Structure of human diferric lactoferrin refined at 2.2 Å resolution
    • [CrossRef] [PubMed]
    • Haridas, M.; Anderson, B.; Baker, E. Structure of human diferric lactoferrin refined at 2.2 Å resolution. Acta Crystallogr. Sect. D Biol. Crystallogr. 1995, 51, 629-646. [CrossRef] [PubMed]
    • (1995) Acta Crystallogr. Sect. D Biol. Crystallogr , vol.51 , pp. 629-646
    • Haridas, M.1    Anderson, B.2    Baker, E.3
  • 52
    • 0030719461 scopus 로고    scopus 로고
    • Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
    • [CrossRef] [PubMed]
    • Moore, S.A.; Anderson, B.F.; Groom, C.R.; Haridas, M.; Baker, E.N. Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution. J. Mol. Biol. 1997, 274, 222-236. [CrossRef] [PubMed]
    • (1997) J. Mol. Biol , vol.274 , pp. 222-236
    • Moore, S.A.1    Anderson, B.F.2    Groom, C.R.3    Haridas, M.4    Baker, E.N.5
  • 53
    • 84904670467 scopus 로고    scopus 로고
    • Breast milk oligosaccharides: Structure-function relationships in the neonate
    • [CrossRef] [PubMed]
    • Smilowitz, J.T.; Lebrilla, C.B.; Mills, D.A.; German, J.B.; Freeman, S.L. Breast milk oligosaccharides: Structure-function relationships in the neonate. Annu. Rev. Nutr. 2014, 34, 143. [CrossRef] [PubMed]
    • (2014) Annu. Rev. Nutr , vol.143 , pp. 34
    • Smilowitz, J.T.1    Lebrilla, C.B.2    Mills, D.A.3    German, J.B.4    Freeman, S.L.5
  • 55
    • 0027052198 scopus 로고
    • Heterogeneity of bovine lactotransferrin glycans. Characterization of α-D-galp-(1→3)-β-D-gal-and _-neuac-(2→6)-_-D-galpnac-(1→4)-β-D-glcnac-substituted N-linked glycans
    • [CrossRef]
    • Coddeville, B.; Strecker, G.; Wieruszeski, J.-M.; Vliegenthart, J.F.; van Halbeek, H.; Peter-Katalinić, J.; Egge, H.; Spik, G. Heterogeneity of bovine lactotransferrin glycans. Characterization of α-D-galp-(1→3)-β-D-gal-and _-neuac-(2→6)-_-D-galpnac-(1→4)-β-D-glcnac-substituted N-linked glycans. Carbohydr. Res. 1992, 236, 145-164. [CrossRef]
    • (1992) Carbohydr. Res , vol.236 , pp. 145-164
    • Coddeville, B.1    Strecker, G.2    Wieruszeski, J.-M.3    Vliegenthart, J.F.4    van Halbeek, H.5    Peter-Katalinić, J.6    Egge, H.7    Spik, G.8
  • 57
    • 48549108366 scopus 로고
    • Structure and function of transferrin
    • [CrossRef]
    • Chung, M. Structure and function of transferrin. Biochem. Educ. 1984, 12, 146-154. [CrossRef]
    • (1984) Biochem. Educ , vol.12 , pp. 146-154
    • Chung, M.1
  • 58
    • 84901920852 scopus 로고    scopus 로고
    • Characterization of goat milk lactoferrin N-glycans and comparison with the N-glycomes of human and bovine milk
    • [CrossRef] [PubMed]
    • Le Parc, A.; Dallas, D.C.; Duaut, S.; Leonil, J.; Martin, P.; Barile, D. Characterization of goat milk lactoferrin N-glycans and comparison with the N-glycomes of human and bovine milk. Electrophoresis 2014, 35, 1560-1570. [CrossRef] [PubMed]
    • (2014) Electrophoresis , vol.35 , pp. 1560-1570
    • Le Parc, A.1    Dallas, D.C.2    Duaut, S.3    Leonil, J.4    Martin, P.5    Barile, D.6
  • 59
    • 85011914742 scopus 로고    scopus 로고
    • Characterization of recombinant human lactoferrin N-glycans expressed in the milk of transgenic cows
    • [CrossRef] [PubMed]
    • Parc, A.L.; Karav, S.; Rouquié, C.; Maga, E.A.; Bunyatratchata, A.; Barile, D. Characterization of recombinant human lactoferrin N-glycans expressed in the milk of transgenic cows. PLoS ONE 2017, 12, e0171477. [CrossRef] [PubMed]
    • (2017) Plos ONE , pp. 12
    • Parc, A.L.1    Karav, S.2    Rouquié, C.3    Maga, E.A.4    Bunyatratchata, A.5    Barile, D.6
  • 61
    • 84860626670 scopus 로고    scopus 로고
    • Comparison of the human and bovine milk N-glycome via high-performance microfluidic chip liquid chromatography and tandem mass spectrometry
    • [CrossRef] [PubMed]
    • Nwosu, C.C.; Aldredge, D.L.; Lee, H.; Lerno, L.A.; Zivkovic, A.M.; German, J.B.; Lebrilla, C.B. Comparison of the human and bovine milk N-glycome via high-performance microfluidic chip liquid chromatography and tandem mass spectrometry. J. Proteome Res. 2012, 11, 2912-2924. [CrossRef] [PubMed]
    • (2012) J. Proteome Res , vol.11 , pp. 2912-2924
    • Nwosu, C.C.1    Aldredge, D.L.2    Lee, H.3    Lerno, L.A.4    Zivkovic, A.M.5    German, J.B.6    Lebrilla, C.B.7
  • 63
    • 0036462598 scopus 로고    scopus 로고
    • Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling
    • [CrossRef] [PubMed]
    • Wormald, M.R.; Petrescu, A.J.; Pao, Y.-L.; Glithero, A.; Elliott, T.; Dwek, R.A. Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling. Chem. Rev. 2002, 102, 371-386. [CrossRef] [PubMed]
    • (2002) Chem. Rev , vol.102 , pp. 371-386
    • Wormald, M.R.1    Petrescu, A.J.2    Pao, Y.-L.3    Glithero, A.4    Elliott, T.5    Dwek, R.A.6
  • 64
    • 84884187149 scopus 로고    scopus 로고
    • Identification and quantification of protein glycosylation
    • [CrossRef]
    • Roth, Z.; Yehezkel, G.; Khalaila, I. Identification and quantification of protein glycosylation. Int. J. Carbohydr. Chem. 2012, 2012, 640923. [CrossRef]
    • (2012) Int. J. Carbohydr. Chem , vol.2012
    • Roth, Z.1    Yehezkel, G.2    Khalaila, I.3
  • 65
    • 84888226286 scopus 로고    scopus 로고
    • Comparison of two approaches for quantitative o-linked glycan analysis used in characterization of recombinant proteins. Anal
    • [CrossRef] [PubMed]
    • Turyan, I.; Hronowski, X.; Sosic, Z.; Lyubarskaya, Y. Comparison of two approaches for quantitative o-linked glycan analysis used in characterization of recombinant proteins. Anal. Biochem. 2014, 446, 28-36. [CrossRef] [PubMed]
    • (2014) Biochem , vol.446 , pp. 28-36
    • Turyan, I.1    Hronowski, X.2    Sosic, Z.3    Lyubarskaya, Y.4
  • 66
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N-and O-linked oligosaccharides from glycoproteins
    • [CrossRef] [PubMed]
    • Patel, T.; Bruce, J.; Merry, A.; Bigge, C.; Wormald, M.; Parekh, R.; Jaques, A. Use of hydrazine to release in intact and unreduced form both N-and O-linked oligosaccharides from glycoproteins. Biochemistry 1993, 32, 679-693. [CrossRef] [PubMed]
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Parekh, R.6    Jaques, A.7
  • 67
    • 0032128332 scopus 로고    scopus 로고
    • Human health perspective of environmental exposure to hydrazines
    • [CrossRef]
    • Choudhary, G.; Hansen, H. Human health perspective of environmental exposure to hydrazines: A review. Chemosphere 1998, 37, 801-843. [CrossRef]
    • (1998) A Review. Chemosphere , vol.37 , pp. 801-843
    • Choudhary, G.1    Hansen, H.2
  • 68
    • 0028926641 scopus 로고
    • Kinetic comparison of peptide: N-glycosidases f and a reveals several differences in substrate specificity
    • [CrossRef] [PubMed]
    • Altmann, F.; Schweiszer, S.; Weber, C. Kinetic comparison of peptide: N-glycosidases f and a reveals several differences in substrate specificity. Glycoconj. J. 1995, 12, 84-93. [CrossRef] [PubMed]
    • (1995) Glycoconj. J , vol.12 , pp. 84-93
    • Altmann, F.1    Schweiszer, S.2    Weber, C.3
  • 69
    • 84877358286 scopus 로고    scopus 로고
    • Isomer-specific LC/MS and LC/MS/MS profiling of the mouse serum N-glycome revealing a number of novel sialylated N-glycans
    • [CrossRef] [PubMed]
    • Hua, S.; Jeong, H.N.; Dimapasoc, L.M.; Kang, I.; Han, C.; Choi, J.-S.; Lebrilla, C.B.; An, H.J. Isomer-specific LC/MS and LC/MS/MS profiling of the mouse serum N-glycome revealing a number of novel sialylated N-glycans. Anal. Chem. 2013, 85, 4636-4643. [CrossRef] [PubMed]
    • (2013) Anal. Chem , vol.85 , pp. 4636-4643
    • Hua, S.1    Jeong, H.N.2    Dimapasoc, L.M.3    Kang, I.4    Han, C.5    Choi, J.-S.6    Lebrilla, C.B.7    An, H.J.8
  • 70
    • 67649229174 scopus 로고    scopus 로고
    • The development of retrosynthetic glycan libraries to profile and classify the human serum N-linked glycome
    • [CrossRef] [PubMed]
    • Kronewitter, S.R.; An, H.J.; De Leoz, M.L.; Lebrilla, C.B.; Miyamoto, S.; Leiserowitz, G.S. The development of retrosynthetic glycan libraries to profile and classify the human serum N-linked glycome. Proteomics 2009, 9, 2986-2994. [CrossRef] [PubMed]
    • (2009) Proteomics , vol.9 , pp. 2986-2994
    • Kronewitter, S.R.1    An, H.J.2    de Leoz, M.L.3    Lebrilla, C.B.4    Miyamoto, S.5    Leiserowitz, G.S.6


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