메뉴 건너뛰기




Volumn 8, Issue 18, 2008, Pages 3833-3847

Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry

Author keywords

Glycoproteins; Human milk proteins; Hydrophilic interaction liquid chromatography; Mass spectrometry; Protective factors

Indexed keywords

GENE PRODUCT; GLYCOPEPTIDASE; GLYCOPROTEIN; OLIGOSACCHARIDE; TRYPSIN;

EID: 53549093906     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200701057     Document Type: Article
Times cited : (124)

References (63)
  • 1
    • 0001623302 scopus 로고
    • Ueber Immunitat dirk verbung und saugung.
    • Ehrlich, P., Ueber Immunitat dirk verbung und saugung. Z. Hyg. Infektionskr. 1892, 12, 183-203.
    • (1892) Z. Hyg. Infektionskr , vol.12 , pp. 183-203
    • Ehrlich, P.1
  • 2
    • 33846953590 scopus 로고    scopus 로고
    • Protection of the neonate by the innate immune system of developing gut and of human milk
    • Newburg, D. S., Walker, W. A., Protection of the neonate by the innate immune system of developing gut and of human milk. Pediatr. Res. 2007, 61, 2-8.
    • (2007) Pediatr. Res , vol.61 , pp. 2-8
    • Newburg, D.S.1    Walker, W.A.2
  • 3
    • 72949100718 scopus 로고    scopus 로고
    • Importance of glycoconjugates in breastfeeding and early nutrition
    • Gardiner, T., Importance of glycoconjugates in breastfeeding and early nutrition. Glycoscience 2000, 1, 1-6.
    • (2000) Glycoscience , vol.1 , pp. 1-6
    • Gardiner, T.1
  • 4
    • 0032980624 scopus 로고    scopus 로고
    • Human milk glycoconjugates that inhibit pathogens
    • Newburg, D. S., Human milk glycoconjugates that inhibit pathogens. Curr. Med. Chem. 1999, 6, 117-27.
    • (1999) Curr. Med. Chem , vol.6 , pp. 117-127
    • Newburg, D.S.1
  • 5
    • 0031845193 scopus 로고    scopus 로고
    • Protective function of proteins and lipids in human milk
    • Hamosh, M., Protective function of proteins and lipids in human milk. Biol. Neonate 1998, 74, 163-76.
    • (1998) Biol. Neonate , vol.74 , pp. 163-176
    • Hamosh, M.1
  • 8
    • 4644332769 scopus 로고    scopus 로고
    • Human milk protective mechanisms
    • Cleary, T. G., Human milk protective mechanisms. Adv. Exp. Med. Biol. 2004, 554, 145-154.
    • (2004) Adv. Exp. Med. Biol , vol.554 , pp. 145-154
    • Cleary, T.G.1
  • 9
    • 33748426813 scopus 로고    scopus 로고
    • Bovine lactoferrin: Benefits and mechanism of action against infections
    • Yamauchi, K., Wakabayashi, H., Shin, K., Takase, M., Bovine lactoferrin: Benefits and mechanism of action against infections. Biochem. Cell Biol. 2006, 84, 291-296.
    • (2006) Biochem. Cell Biol , vol.84 , pp. 291-296
    • Yamauchi, K.1    Wakabayashi, H.2    Shin, K.3    Takase, M.4
  • 10
    • 0029080953 scopus 로고
    • Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro
    • Harmsen, M. C., Swart, P. J., de Béthune, M. P., Pauwels, R. et al., Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J. Infect. Dis. 1995, 172, 380-388.
    • (1995) J. Infect. Dis , vol.172 , pp. 380-388
    • Harmsen, M.C.1    Swart, P.J.2    de Béthune, M.P.3    Pauwels, R.4
  • 11
    • 0021985763 scopus 로고
    • Protective factors in milk and the development of the immune system
    • Hanson, L. A., Ahlstedt, S., Andersson, B., Carlsson, B. et al., Protective factors in milk and the development of the immune system. Pediatrics 1985, 75, 172-176.
    • (1985) Pediatrics , vol.75 , pp. 172-176
    • Hanson, L.A.1    Ahlstedt, S.2    Andersson, B.3    Carlsson, B.4
  • 13
    • 0031844095 scopus 로고    scopus 로고
    • Glycoproteins of the human milk fat globule in the protection of the breast-fed infant against infections
    • Peterson, J. A., Patton, S., Hamosh, M., Glycoproteins of the human milk fat globule in the protection of the breast-fed infant against infections. Biol. Neonate 1998, 74, 143-162.
    • (1998) Biol. Neonate , vol.74 , pp. 143-162
    • Peterson, J.A.1    Patton, S.2    Hamosh, M.3
  • 14
    • 0025260978 scopus 로고
    • Adhesins as lectins: Specificity and role in infection
    • Ofek, I., Sharon, N., Adhesins as lectins: Specificity and role in infection. Curr. Top. Microbiol. Immunol. 1990, 151, 91-113.
    • (1990) Curr. Top. Microbiol. Immunol , vol.151 , pp. 91-113
    • Ofek, I.1    Sharon, N.2
  • 15
    • 0022643495 scopus 로고
    • Lectin binding affinities of human milk fat globule (HMFG) membrane antigens
    • Ashorn, P., Vilja, P., Shorn, R., Rohn, K., Lectin binding affinities of human milk fat globule (HMFG) membrane antigens. Mol. Immunol. 1986, 23, 221-230.
    • (1986) Mol. Immunol , vol.23 , pp. 221-230
    • Ashorn, P.1    Vilja, P.2    Shorn, R.3    Rohn, K.4
  • 17
    • 0034699356 scopus 로고    scopus 로고
    • Glycoprotein degradation: Do sugars hold the key?
    • Frigerio, L., Lord, J. M., Glycoprotein degradation: Do sugars hold the key? Curr. Biol. 2000, 10, R 674-677.
    • (2000) Curr. Biol , vol.10 , Issue.R , pp. 674-677
    • Frigerio, L.1    Lord, J.M.2
  • 18
    • 0037083451 scopus 로고    scopus 로고
    • Use of proteomic methodology for the characterization of human milk fat globular membrane proteins
    • Charlwood, J., Hanrahan, S., Tyldesley, R., Langridge, J. et al., Use of proteomic methodology for the characterization of human milk fat globular membrane proteins. Anal. Biochem. 2002, 301, 314-324.
    • (2002) Anal. Biochem , vol.301 , pp. 314-324
    • Charlwood, J.1    Hanrahan, S.2    Tyldesley, R.3    Langridge, J.4
  • 19
    • 1642301670 scopus 로고    scopus 로고
    • Casein proteolysis in human milk: Tracing the pattern of casein breakdown and the formation of potential bioactive peptides
    • Ferranti, P., Traisci, M. V., Picariello, G., Nasi, A. et al., Casein proteolysis in human milk: Tracing the pattern of casein breakdown and the formation of potential bioactive peptides. J. Dairy Res. 2004, 7, 74-87.
    • (2004) J. Dairy Res , vol.7 , pp. 74-87
    • Ferranti, P.1    Traisci, M.V.2    Picariello, G.3    Nasi, A.4
  • 20
    • 33645670516 scopus 로고    scopus 로고
    • Human colostrum: Identification of minor proteins in the aqueous phase by proteomics
    • Palmer, D. J., Kelly, V. C., Smit, A. M., Kuy, S. et al., Human colostrum: Identification of minor proteins in the aqueous phase by proteomics. Proteomics 2006, 6, 2208-2216.
    • (2006) Proteomics , vol.6 , pp. 2208-2216
    • Palmer, D.J.1    Kelly, V.C.2    Smit, A.M.3    Kuy, S.4
  • 21
    • 0036107938 scopus 로고    scopus 로고
    • Identification of low-abundance proteins of bovine colostral and mature milk using two-dimensional electrophoresis followed by microsequencing and mass spectrometry
    • Yamada, M., Murakami, K., Wallingford, J. C., Yuki, Y., Identification of low-abundance proteins of bovine colostral and mature milk using two-dimensional electrophoresis followed by microsequencing and mass spectrometry. Electrophoresis 2002, 23, 1153-1160.
    • (2002) Electrophoresis , vol.23 , pp. 1153-1160
    • Yamada, M.1    Murakami, K.2    Wallingford, J.C.3    Yuki, Y.4
  • 22
    • 20144383119 scopus 로고    scopus 로고
    • High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry
    • Zhang, H., Yi, E. C., Li, X. J., Mallick, P. et al., High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry. Mol. Cell. Proteomics 2005, 4, 144-155.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 144-155
    • Zhang, H.1    Yi, E.C.2    Li, X.J.3    Mallick, P.4
  • 23
    • 33745000741 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry
    • Ramachandran, P., Boontheung, P., Xie, Y., Sondej, M. et al., Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J. Proteome Res. 2006, 5, 1493-1503.
    • (2006) J. Proteome Res , vol.5 , pp. 1493-1503
    • Ramachandran, P.1    Boontheung, P.2    Xie, Y.3    Sondej, M.4
  • 24
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg, J., Pilch, B. J., Podtelejnikov, A. V., Wiśniewski, J. R., Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 2004, 4, 454-465.
    • (2004) Proteomics , vol.4 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wiśniewski, J.R.4
  • 25
    • 33646873090 scopus 로고    scopus 로고
    • Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electro-spray linear ion trap-Fourier transform mass spectrometry
    • Wang, Y., Wu, S. L., Hancock, W. S., Approaches to the study of N-linked glycoproteins in human plasma using lectin affinity chromatography and nano-HPLC coupled to electro-spray linear ion trap-Fourier transform mass spectrometry. Glycobiology 2006, 16, 514-523.
    • (2006) Glycobiology , vol.16 , pp. 514-523
    • Wang, Y.1    Wu, S.L.2    Hancock, W.S.3
  • 26
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H., Li, X. J., Martin, D. B., Aebersold, R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 2003, 21, 660-666.
    • (2003) Nat. Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 27
    • 33746542437 scopus 로고    scopus 로고
    • Isolation of glycoproteins and identification of their N-linked glycosylation sites
    • Zhang, H., Aebersold, R., Isolation of glycoproteins and identification of their N-linked glycosylation sites. Methods Mol. Biol. 2006, 328, 177-185.
    • (2006) Methods Mol. Biol , vol.328 , pp. 177-185
    • Zhang, H.1    Aebersold, R.2
  • 28
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., Roepstorff, P., A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J. Proteome Res. 2004, 3, 556-566.
    • (2004) J. Proteome Res , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 29
    • 33751300966 scopus 로고    scopus 로고
    • Simple separation of isomeric sialylated N-glycopeptides by a zwitterionic type of hydrophilic interaction chromatography
    • Takegawa, Y., Deguchi, K., Ito, H., Keira, T. et al., Simple separation of isomeric sialylated N-glycopeptides by a zwitterionic type of hydrophilic interaction chromatography. J. Sep. Sci. 2006, 29, 2533-2540.
    • (2006) J. Sep. Sci , vol.29 , pp. 2533-2540
    • Takegawa, Y.1    Deguchi, K.2    Ito, H.3    Keira, T.4
  • 30
    • 23844499696 scopus 로고    scopus 로고
    • A rapid sample preparation method for mass spectrometric characterization of N-linked glycans
    • Yu, Y. Q., Gilar, M., Kaska, J., Gebier, J. C., A rapid sample preparation method for mass spectrometric characterization of N-linked glycans. Rapid Commun. Mass Spectrom. 2005, 19, 2331-2336.
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 2331-2336
    • Yu, Y.Q.1    Gilar, M.2    Kaska, J.3    Gebier, J.C.4
  • 31
    • 4644220718 scopus 로고    scopus 로고
    • Human milk proteins: Key components for the biological activity of human milk
    • Lönnerdal, B., Human milk proteins: Key components for the biological activity of human milk. Adv. Exp. Med. Biol. 2004, 554, 11-25.
    • (2004) Adv. Exp. Med. Biol , vol.554 , pp. 11-25
    • Lönnerdal, B.1
  • 32
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R., Roepstorff, P., Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 1999, 34, 105-116.
    • (1999) J. Mass Spectrom , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 34
    • 0023833884 scopus 로고
    • Chemical structure of neutral sugar chains isolated from human mature milk kappacasein
    • Saito, T., Itoh, T., Adachi, S., Chemical structure of neutral sugar chains isolated from human mature milk kappacasein. Biochim. Biophys. Acta 1988, 964, 213-220.
    • (1988) Biochim. Biophys. Acta , vol.964 , pp. 213-220
    • Saito, T.1    Itoh, T.2    Adachi, S.3
  • 36
    • 4143092643 scopus 로고    scopus 로고
    • The proteomic approach to analysis of human milk fat globule membrane
    • Cavaletto, M., Giuffrida, M. G., Conti, A., The proteomic approach to analysis of human milk fat globule membrane. Clin. Chim Acta 2004, 347, 41-48.
    • (2004) Clin. Chim Acta , vol.347 , pp. 41-48
    • Cavaletto, M.1    Giuffrida, M.G.2    Conti, A.3
  • 37
    • 10744229391 scopus 로고    scopus 로고
    • Structural protome of human colostral fat globule membrane proteins
    • Fortunato, D., Giuffrida, M. G., Cavaletto, M., Garoffo, L. P. et al., Structural protome of human colostral fat globule membrane proteins. Proteomics 2003, 3, 897-905.
    • (2003) Proteomics , vol.3 , pp. 897-905
    • Fortunato, D.1    Giuffrida, M.G.2    Cavaletto, M.3    Garoffo, L.P.4
  • 38
    • 32344447939 scopus 로고    scopus 로고
    • Characterization of the mouse brain proteome using global proteomic analysis complemented with cysteinyl-peptide enrichment
    • Wang, H., Qian, W. J., Chin, M. H., Petyuk, V. A. et al., Characterization of the mouse brain proteome using global proteomic analysis complemented with cysteinyl-peptide enrichment. J. Proteome Res. 2006, 5, 361-369.
    • (2006) J. Proteome Res , vol.5 , pp. 361-369
    • Wang, H.1    Qian, W.J.2    Chin, M.H.3    Petyuk, V.A.4
  • 39
    • 33745090847 scopus 로고    scopus 로고
    • Depletion efficiency and recovery of trace markers from a multiparameter immunodepletion column
    • Brand, J., Haslberger, T., Zolg, W., Pestlin, G., Palme, S., Depletion efficiency and recovery of trace markers from a multiparameter immunodepletion column. Proteomics 2006, 6, 3236-3242.
    • (2006) Proteomics , vol.6 , pp. 3236-3242
    • Brand, J.1    Haslberger, T.2    Zolg, W.3    Pestlin, G.4    Palme, S.5
  • 40
    • 14344257501 scopus 로고    scopus 로고
    • Harvey, D. J., Proteomic analysis of glycosylation: Structural determination of N- and O-linked glycans by mass spectrometry. Expert Rev. Proteomics 2005, 2, 87-101.
    • Harvey, D. J., Proteomic analysis of glycosylation: Structural determination of N- and O-linked glycans by mass spectrometry. Expert Rev. Proteomics 2005, 2, 87-101.
  • 41
    • 0030873812 scopus 로고    scopus 로고
    • Differential splicing of pre-messenger RNA produces multiple forms of mature caprine αs1-casein
    • Ferranti, P., Addeo, F., Malorni, A., Chianese, L. et al., Differential splicing of pre-messenger RNA produces multiple forms of mature caprine αs1-casein. Eur. J. Biochem. 1997, 249, 1-7.
    • (1997) Eur. J. Biochem , vol.249 , pp. 1-7
    • Ferranti, P.1    Addeo, F.2    Malorni, A.3    Chianese, L.4
  • 42
    • 18244405829 scopus 로고    scopus 로고
    • Inter-allelic recombination is probably responsible for the occurrence of a new alpha(s1)-casein variant found in the goat species
    • Bevilacqua, C., Ferranti, P., Garro, G., Veltri, C. et al., Inter-allelic recombination is probably responsible for the occurrence of a new alpha(s1)-casein variant found in the goat species. Eur. J. Biochem. 2002, 269, 1293-1303.
    • (2002) Eur. J. Biochem , vol.269 , pp. 1293-1303
    • Bevilacqua, C.1    Ferranti, P.2    Garro, G.3    Veltri, C.4
  • 43
    • 33746570234 scopus 로고    scopus 로고
    • Analysis of posttranslational modifications of proteins by tandem mass spectrometry
    • Larsen, M. R., Trelle, M. B., Thingholm, T. E., Jensen, O. N., Analysis of posttranslational modifications of proteins by tandem mass spectrometry. Biotechniques 2006, 40, 790-798.
    • (2006) Biotechniques , vol.40 , pp. 790-798
    • Larsen, M.R.1    Trelle, M.B.2    Thingholm, T.E.3    Jensen, O.N.4
  • 44
    • 0030866216 scopus 로고    scopus 로고
    • Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) glycosylation motifs
    • Vance, B. A., Wu, W., Ribaudo, R. K., Segal, D. M., Kearse, K. P., Multiple dimeric forms of human CD69 result from differential addition of N-glycans to typical (Asn-X-Ser/Thr) and atypical (Asn-X-Cys) glycosylation motifs. J. Biol. Chem. 1997, 272, 23117-23122.
    • (1997) J. Biol. Chem , vol.272 , pp. 23117-23122
    • Vance, B.A.1    Wu, W.2    Ribaudo, R.K.3    Segal, D.M.4    Kearse, K.P.5
  • 45
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y., von Heijne, G., Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng. 1990, 3, 433-442.
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    von Heijne, G.2
  • 46
    • 33846623696 scopus 로고    scopus 로고
    • Characterisation of host defence proteins in milk using a proteomic approach
    • Smolenski, G., Haines, S., Kwan, F. Y., Bond, J. et al., Characterisation of host defence proteins in milk using a proteomic approach. J. Proteome Res. 2007, 6, 207-215.
    • (2007) J. Proteome Res , vol.6 , pp. 207-215
    • Smolenski, G.1    Haines, S.2    Kwan, F.Y.3    Bond, J.4
  • 47
    • 0017097407 scopus 로고
    • Total protein and immunoglobulin content of human milk
    • Donat, H., Total protein and immunoglobulin content of human milk. Zentralbl. Gynakol. 1976, 98, 1631-1637.
    • (1976) Zentralbl. Gynakol , vol.98 , pp. 1631-1637
    • Donat, H.1
  • 48
    • 0032542960 scopus 로고    scopus 로고
    • Role of human-milk lactadherin in protection against symptomatic rotavirus infection
    • Newburg, D. S., Peterson, J. A., Ruiz-Palacios, G. M., Role of human-milk lactadherin in protection against symptomatic rotavirus infection. Lancet 1998, 351, 1160-1164.
    • (1998) Lancet , vol.351 , pp. 1160-1164
    • Newburg, D.S.1    Peterson, J.A.2    Ruiz-Palacios, G.M.3
  • 49
    • 0030806667 scopus 로고    scopus 로고
    • The unusual amino acid triplet Asn-lle-Cys is a glycosylation consensus site in human α-lactalbumin
    • Giuffrida, M. G., Cavaletto, M., Giunta, C., Neuteboom, B. et al., The unusual amino acid triplet Asn-lle-Cys is a glycosylation consensus site in human α-lactalbumin. J. Prot. Chem. 1997, 16, 747-753.
    • (1997) J. Prot. Chem , vol.16 , pp. 747-753
    • Giuffrida, M.G.1    Cavaletto, M.2    Giunta, C.3    Neuteboom, B.4
  • 50
    • 0031728646 scopus 로고    scopus 로고
    • Identification of minor proteins of human colostrum and mature milk by two-dimensional electrophoresis
    • Murakami, K., Lagarde, M., Yuki, Y., Identification of minor proteins of human colostrum and mature milk by two-dimensional electrophoresis. Electrophoresis 1998, 19, 2521-2527.
    • (1998) Electrophoresis , vol.19 , pp. 2521-2527
    • Murakami, K.1    Lagarde, M.2    Yuki, Y.3
  • 51
    • 0346797301 scopus 로고
    • Identification of the macrophage mannose receptor as a 175-kDa membrane protein
    • Wileman, T. E., Lennartz, M. R., Stahl, D. P., Identification of the macrophage mannose receptor as a 175-kDa membrane protein. Proc. Nati. Acad. Sci. USA 1986, 83, 2501-2505.
    • (1986) Proc. Nati. Acad. Sci. USA , vol.83 , pp. 2501-2505
    • Wileman, T.E.1    Lennartz, M.R.2    Stahl, D.P.3
  • 52
    • 0020404378 scopus 로고
    • Isolation, characterization, and comparison of the solubilized particulate and soluble folate binding proteins from human milk
    • Antony, A. C., Utley, C. S., Marcell, P. D., Kolhouse, J. F., Isolation, characterization, and comparison of the solubilized particulate and soluble folate binding proteins from human milk. J. Biol. Chem. 1982, 257, 10081-10089.
    • (1982) J. Biol. Chem , vol.257 , pp. 10081-10089
    • Antony, A.C.1    Utley, C.S.2    Marcell, P.D.3    Kolhouse, J.F.4
  • 53
    • 0037901694 scopus 로고    scopus 로고
    • Nutritional and physiologic significance of human milk proteins
    • Lönnerdal, B., Nutritional and physiologic significance of human milk proteins. Am. J. Clin. Nutr. 2003, 77, 1537S-1543S.
    • (2003) Am. J. Clin. Nutr , vol.77
    • Lönnerdal, B.1
  • 54
    • 0029093896 scopus 로고
    • Shedding and enrichment of the glycolipid-anchored complement lysis inhibitor protectin (CD59) into milk fat globules
    • Hakulinen, J., Meri, S., Shedding and enrichment of the glycolipid-anchored complement lysis inhibitor protectin (CD59) into milk fat globules. Immunology 1995, 85, 495-501.
    • (1995) Immunology , vol.85 , pp. 495-501
    • Hakulinen, J.1    Meri, S.2
  • 55
    • 0028962198 scopus 로고
    • Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments
    • Jones, P. L., Boudreau, N., Myers, C. A., Erickson, H. P., Bissen, M. J., Tenascin-C inhibits extracellular matrix-dependent gene expression in mammary epithelial cells. Localization of active regions using recombinant tenascin fragments. J. Cell Sci. 1995, 108, 519-527.
    • (1995) J. Cell Sci , vol.108 , pp. 519-527
    • Jones, P.L.1    Boudreau, N.2    Myers, C.A.3    Erickson, H.P.4    Bissen, M.J.5
  • 56
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu, T., Qian, W. J., Gritsenko, M. A., Camp, D. G., Il et al., Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 2005, 4, 2070-2080.
    • (2005) J. Proteome Res , vol.4 , pp. 2070-2080
    • Liu, T.1    Qian, W.J.2    Gritsenko, M.A.3    Camp, D.G.4    Il5
  • 57
    • 33748788003 scopus 로고    scopus 로고
    • Deamidation of-Asn-Gly- Sequences during Sample Preparation for Proteomics: Consequences for MALDI and HPLC-MALDI Analysis
    • Krokhin, O. V., Antonovici, M., Ens, W., Wilkins, J. A., Standing, K. G., Deamidation of-Asn-Gly- Sequences during Sample Preparation for Proteomics: Consequences for MALDI and HPLC-MALDI Analysis. Anal. Chem. 2006; 78, 6645-6650.
    • (2006) Anal. Chem , vol.78 , pp. 6645-6650
    • Krokhin, O.V.1    Antonovici, M.2    Ens, W.3    Wilkins, J.A.4    Standing, K.G.5
  • 59
    • 0033106490 scopus 로고    scopus 로고
    • 18O-Iabeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching
    • 18O-Iabeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching. Anal. Chem. 1999, 71, 1431-1440.
    • (1999) Anal. Chem , vol.71 , pp. 1431-1440
    • Küster, B.1    Mann, M.2
  • 60
    • 0022762750 scopus 로고
    • Structure identification of the complex-type, asparagine- linked sugar chains of beta-D-galactosyl- transferase purified from human milk
    • Endo, T., Amano, J., Berger, E. G., Kobata, A., Structure identification of the complex-type, asparagine- linked sugar chains of beta-D-galactosyl- transferase purified from human milk. Carbohydr. Res. 1986, 150, 241-263.
    • (1986) Carbohydr. Res , vol.150 , pp. 241-263
    • Endo, T.1    Amano, J.2    Berger, E.G.3    Kobata, A.4
  • 61
    • 0035701463 scopus 로고    scopus 로고
    • MUC1 and MUC-X, epithelial mucins of breast and milk
    • Patton, S., MUC1 and MUC-X, epithelial mucins of breast and milk. Adv. Exp. Med. Biol. 2001, 501, 35-45.
    • (2001) Adv. Exp. Med. Biol , vol.501 , pp. 35-45
    • Patton, S.1
  • 62
    • 0035701947 scopus 로고    scopus 로고
    • Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane
    • Peterson, J. A., Scallan, C. D., Ceriani, R. L., Hamosh, M., Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane. Adv. Exp. Med. Biol. 2001, 501, 179-187.
    • (2001) Adv. Exp. Med. Biol , vol.501 , pp. 179-187
    • Peterson, J.A.1    Scallan, C.D.2    Ceriani, R.L.3    Hamosh, M.4
  • 63
    • 0030830164 scopus 로고    scopus 로고
    • Localization of O-glycosylation sites on glycopeptide fragments from lactation associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo
    • Müller, S., Goletz, S., Packer, N., Gooley, A. A. et al., Localization of O-glycosylation sites on glycopeptide fragments from lactation associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo. J. Biol. Chem. 1997, 272, 24780-24793.
    • (1997) J. Biol. Chem , vol.272 , pp. 24780-24793
    • Müller, S.1    Goletz, S.2    Packer, N.3    Gooley, A.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.