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Volumn 48, Issue 7, 2013, Pages 779-794

Through the eye of an electrospray needle: Mass spectrometric identification of the major peptides and proteins in the milk of the one-humped camel (Camelus dromedarius)

Author keywords

camel milk; Camelus dromedarius; DIGE; mass spectrometry; peptides; proteins; proteomics

Indexed keywords

CAMEL MILKS; CAMELUS DROMEDARIUS; DIGE; LIQUID CHROMATOGRAPHY TANDEM MASS SPECTROMETRY (LC MS/MS); MASS SPECTROMETRIC IDENTIFICATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEOMICS; TWO-DIMENSIONAL GEL ELECTROPHORESIS;

EID: 84879969506     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.3213     Document Type: Article
Times cited : (21)

References (64)
  • 3
    • 84858141316 scopus 로고    scopus 로고
    • Camel milk modulates the expression of aryl hydrocarbon receptor-regulated genes, Cyp1a1, Nqo1, and Gsta1, in murine hepatoma Hepa 1c1c7 cells
    • H. M. Korashy, M. A. El Gendy, A. A. Alhaider, A. O. El-Kadi,. Camel milk modulates the expression of aryl hydrocarbon receptor-regulated genes, Cyp1a1, Nqo1, and Gsta1, in murine hepatoma Hepa 1c1c7 cells. J. Biomed. Biotechnol. 2012, 2012, 782642.
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 782642
    • Korashy, H.M.1    El Gendy, M.A.2    Alhaider, A.A.3    El-Kadi, A.O.4
  • 4
    • 84862298988 scopus 로고    scopus 로고
    • Camel milk triggers apoptotic signaling pathways in human hepatoma HepG2 and breast cancer MCF7 cell lines through transcriptional mechanism
    • H. M. Korashy, Z. H. Maayah, A. R. Abd-Allah, A. O. El-Kadi, A. A. Alhaider,. Camel milk triggers apoptotic signaling pathways in human hepatoma HepG2 and breast cancer MCF7 cell lines through transcriptional mechanism. J. Biomed. Biotechnol. 2012, 2012, 593195.
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 593195
    • Korashy, H.M.1    Maayah, Z.H.2    Abd-Allah, A.R.3    El-Kadi, A.O.4    Alhaider, A.A.5
  • 6
    • 0020023599 scopus 로고
    • Mechanism of the therapeutic action of whole mare's and camel's milk in chronic hepatitis
    • T. Sharmanov, A. K. Zhangabylov, R. D. Zhaksylykova,. Mechanism of the therapeutic action of whole mare's and camel's milk in chronic hepatitis. Vopr. Pitan. 1982, 17.
    • (1982) Vopr. Pitan. , pp. 17
    • Sharmanov, T.1    Zhangabylov, A.K.2    Zhaksylykova, R.D.3
  • 8
    • 34347394504 scopus 로고    scopus 로고
    • Camel lactoferrin markedly inhibits hepatitis C virus genotype 4 infection of human peripheral blood leukocytes
    • R. M. Redwan el, A. Tabll,. Camel lactoferrin markedly inhibits hepatitis C virus genotype 4 infection of human peripheral blood leukocytes. J. Immunoassay Immunochem. 2007, 28, 267.
    • (2007) J. Immunoassay Immunochem. , vol.28 , pp. 267
    • Redwan El, R.M.1    Tabll, A.2
  • 9
    • 84857075449 scopus 로고    scopus 로고
    • Inhibitory effects of native and recombinant full-length camel lactoferrin and its N and C lobes on hepatitis C virus infection of Huh7.5 cells
    • Y. Liao, E. El-Fakkarany, B. Lonnerdal, E. M. Redwan,. Inhibitory effects of native and recombinant full-length camel lactoferrin and its N and C lobes on hepatitis C virus infection of Huh7.5 cells. J. Med. Microbiol. 2012, 61, 375.
    • (2012) J. Med. Microbiol. , vol.61 , pp. 375
    • Liao, Y.1    El-Fakkarany, E.2    Lonnerdal, B.3    Redwan, E.M.4
  • 10
    • 0019564788 scopus 로고
    • Effectiveness of peptic ulcer diet therapy using rations containing whole mare's and camel's milk
    • T. Sharmanov, R. Kadyrova, B. A. Salkhanov,. Effectiveness of peptic ulcer diet therapy using rations containing whole mare's and camel's milk. Vopr. Pitan. 1981, 10.
    • (1981) Vopr. Pitan. , pp. 10
    • Sharmanov, T.1    Kadyrova, R.2    Salkhanov, B.A.3
  • 17
    • 18044376224 scopus 로고    scopus 로고
    • Camel milk as an adjunct to insulin therapy improves long-term glycemic control and reduction in doses of insulin in patients with type-1 diabetes A 1 year randomized controlled trial
    • R. P. Agrawal, R. Beniwal, D. K. Kochar, F. C. Tuteja, S. K. Ghorui, M. S. Sahani, S. Sharma,. Camel milk as an adjunct to insulin therapy improves long-term glycemic control and reduction in doses of insulin in patients with type-1 diabetes A 1 year randomized controlled trial. Diabetes Res. Clin. Pract. 2005, 68, 176.
    • (2005) Diabetes Res. Clin. Pract. , vol.68 , pp. 176
    • Agrawal, R.P.1    Beniwal, R.2    Kochar, D.K.3    Tuteja, F.C.4    Ghorui, S.K.5    Sahani, M.S.6    Sharma, S.7
  • 20
    • 0027689121 scopus 로고
    • Composition and characteristics of camel milk
    • Z. Farah,. Composition and characteristics of camel milk. J. Dairy Res. 1993, 60, 603.
    • (1993) J. Dairy Res. , vol.60 , pp. 603
    • Farah, Z.1
  • 21
    • 0034985955 scopus 로고    scopus 로고
    • Fatty acids and lipids of camel milk and colostrum
    • A. M. Gorban, O. M. Izzeldin,. Fatty acids and lipids of camel milk and colostrum. Int. J. Food Sci. Nutr. 2001, 52, 283.
    • (2001) Int. J. Food Sci. Nutr. , vol.52 , pp. 283
    • Gorban, A.M.1    Izzeldin, O.M.2
  • 23
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • D. A. Clare, H. E. Swaisgood,. Bioactive milk peptides: a prospectus. J. Dairy Sci. 2000, 83, 1187.
    • (2000) J. Dairy Sci. , vol.83 , pp. 1187
    • Clare, D.A.1    Swaisgood, H.E.2
  • 25
    • 49749143329 scopus 로고    scopus 로고
    • Beta-lactoglobulin as source of bioactive peptides
    • B. Hernandez-Ledesma, I. Recio, L. Amigo,. Beta-lactoglobulin as source of bioactive peptides. Amino Acids 2008, 35, 257.
    • (2008) Amino Acids , vol.35 , pp. 257
    • Hernandez-Ledesma, B.1    Recio, I.2    Amigo, L.3
  • 26
    • 0032861381 scopus 로고    scopus 로고
    • Bioactive peptides encrypted in milk proteins: Proteolytic activation and thropho-functional properties
    • H. Meisel, W. Bockelmann,. Bioactive peptides encrypted in milk proteins: proteolytic activation and thropho-functional properties. Antonie Van Leeuwenhoek 1999, 76, 207.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 207
    • Meisel, H.1    Bockelmann, W.2
  • 30
    • 84984458687 scopus 로고
    • Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects
    • E. Schlimme, H. Meisel,. Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects. Nahrung 1995, 39, 1.
    • (1995) Nahrung , vol.39 , pp. 1
    • Schlimme, E.1    Meisel, H.2
  • 31
    • 0037307257 scopus 로고    scopus 로고
    • A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects
    • L. Seppo, T. Jauhiainen, T. Poussa, R. Korpela,. A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects. Am. J. Clin. Nutr. 2003, 77, 326.
    • (2003) Am. J. Clin. Nutr. , vol.77 , pp. 326
    • Seppo, L.1    Jauhiainen, T.2    Poussa, T.3    Korpela, R.4
  • 35
    • 0032412018 scopus 로고    scopus 로고
    • Breastfeeding provides passive and likely long-lasting active immunity
    • L. A. Hanson,. Breastfeeding provides passive and likely long-lasting active immunity. Ann. Allergy Asthma Immunol. 1998, 81, 523.
    • (1998) Ann. Allergy Asthma Immunol. , vol.81 , pp. 523
    • Hanson, L.A.1
  • 36
    • 0032830777 scopus 로고    scopus 로고
    • Passive immunity against rotavirus in infants
    • L. Hammarstrom,. Passive immunity against rotavirus in infants. Acta Paediatr. Suppl. 1999, 88, 127.
    • (1999) Acta Paediatr. Suppl. , vol.88 , pp. 127
    • Hammarstrom, L.1
  • 38
    • 0034494496 scopus 로고    scopus 로고
    • Bovine milk antibodies for health
    • H. Korhonen, P. Marnila, H. S. Gill,. Bovine milk antibodies for health. Br. J. Nutr. 2000, 84 (Suppl 1), S135.
    • (2000) Br. J. Nutr. , vol.84 , Issue.SUPPL. 1
    • Korhonen, H.1    Marnila, P.2    Gill, H.S.3
  • 39
    • 18344398300 scopus 로고    scopus 로고
    • Passive acquired immunity against measles in infants born to naturally infected and vaccinated mothers
    • L. Szenborn, A. Tischer, J. Pejcz, Z. Rudkowski, M. Wojcik,. Passive acquired immunity against measles in infants born to naturally infected and vaccinated mothers. Med. Sci. Monit. 2003, 9, CR541.
    • (2003) Med. Sci. Monit. , vol.9
    • Szenborn, L.1    Tischer, A.2    Pejcz, J.3    Rudkowski, Z.4    Wojcik, M.5
  • 40
    • 70350432951 scopus 로고    scopus 로고
    • Antibody-mediated protection against infection with helicobacter pylori in a suckling mouse model of passive immunity
    • R. J. Gorrell, R. M. Robins-Browne,. Antibody-mediated protection against infection with helicobacter pylori in a suckling mouse model of passive immunity. Infect. Immun. 2009, 77, 5116.
    • (2009) Infect. Immun. , vol.77 , pp. 5116
    • Gorrell, R.J.1    Robins-Browne, R.M.2
  • 42
    • 41149161152 scopus 로고    scopus 로고
    • Gel-eluted liquid fraction entrapment electrophoresis: An electrophoretic method for broad molecular weight range proteome separation
    • J. C. Tran, A. A. Doucette,. Gel-eluted liquid fraction entrapment electrophoresis: an electrophoretic method for broad molecular weight range proteome separation. Anal. Chem. 2008, 80, 1568.
    • (2008) Anal. Chem. , vol.80 , pp. 1568
    • Tran, J.C.1    Doucette, A.A.2
  • 43
    • 68049099249 scopus 로고    scopus 로고
    • Multiplexed size separation of intact proteins in solution phase for mass spectrometry
    • J. C. Tran, A. A. Doucette,. Multiplexed size separation of intact proteins in solution phase for mass spectrometry. Anal. Chem. 2009, 81, 6201.
    • (2009) Anal. Chem. , vol.81 , pp. 6201
    • Tran, J.C.1    Doucette, A.A.2
  • 44
    • 42349113800 scopus 로고    scopus 로고
    • Parallel electrophoretic depletion, fractionation, concentration, and desalting of 96 complex biological samples for mass spectrometry
    • 2nd
    • J. B. t. Harkins, B. B. Katz, S. J. Pastor, P. Osucha, D. G. Hafeman, C. E. Witkowski, 2nd, J. L. Norris,. Parallel electrophoretic depletion, fractionation, concentration, and desalting of 96 complex biological samples for mass spectrometry. Anal. Chem. 2008, 80, 2734.
    • (2008) Anal. Chem. , vol.80 , pp. 2734
    • Harkins, J.B.T.1    Katz, B.B.2    Pastor, S.J.3    Osucha, P.4    Hafeman, D.G.5    Witkowski, C.E.6    Norris, J.L.7
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. M. Bradford,. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 46
    • 45849147682 scopus 로고    scopus 로고
    • Bioactive peptides and proteins from foods: Indication for health effects
    • N. P. Moller, K. E. Scholz-Ahrens, N. Roos, J. Schrezenmeir,. Bioactive peptides and proteins from foods: indication for health effects. Eur. J. Nutr. 2008, 47, 171.
    • (2008) Eur. J. Nutr. , vol.47 , pp. 171
    • Moller, N.P.1    Scholz-Ahrens, K.E.2    Roos, N.3    Schrezenmeir, J.4
  • 47
    • 57749118622 scopus 로고    scopus 로고
    • Comparative study on heat stability and functionality of camel and bovine milk whey proteins
    • L. C. Laleye, B. Jobe, A. A. Wasesa,. Comparative study on heat stability and functionality of camel and bovine milk whey proteins. J. Dairy Sci. 2008, 91, 4527.
    • (2008) J. Dairy Sci. , vol.91 , pp. 4527
    • Laleye, L.C.1    Jobe, B.2    Wasesa, A.A.3
  • 49
    • 84861612118 scopus 로고    scopus 로고
    • Comparison of the hydrolysis of bovine kappa-casein by camel and bovine chymosin: A kinetic and specificity study
    • K. K. Moller, F. P. Rattray, J. C. Sorensen, Y. Ardo,. Comparison of the hydrolysis of bovine kappa-casein by camel and bovine chymosin: a kinetic and specificity study. J. Agric. Food Chem. 2012, 60, 5454.
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 5454
    • Moller, K.K.1    Rattray, F.P.2    Sorensen, J.C.3    Ardo, Y.4
  • 50
    • 33645418473 scopus 로고    scopus 로고
    • Indigenous proteolytic enzymes in milk: A brief overview of the present state of knowledge
    • A. L. Kelly, F. O'Flaherty, P. F. Fox,. Indigenous proteolytic enzymes in milk: A brief overview of the present state of knowledge. Int. Dairy J. 2006, 16, 563.
    • (2006) Int. Dairy J. , vol.16 , pp. 563
    • Kelly, A.L.1    O'Flaherty, F.2    Fox, P.F.3
  • 51
    • 0022261490 scopus 로고
    • Isolation of a specific mu-opiate receptor peptide, morphiceptin, from an enzymatic digest of milk proteins
    • K. J. Chang, Y. F. Su, D. A. Brent, J. K. Chang,. Isolation of a specific mu-opiate receptor peptide, morphiceptin, from an enzymatic digest of milk proteins. J. Biol. Chem. 1985, 260, 9706.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9706
    • Chang, K.J.1    Su, Y.F.2    Brent, D.A.3    Chang, J.K.4
  • 52
    • 0029924099 scopus 로고    scopus 로고
    • Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins
    • H. Kayser, H. Meisel,. Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Lett. 1996, 383, 18.
    • (1996) FEBS Lett. , vol.383 , pp. 18
    • Kayser, H.1    Meisel, H.2
  • 54
  • 55
    • 0038397146 scopus 로고    scopus 로고
    • Food-derived bioactive peptides-opportunities for designing future foods
    • H. Korhonen, A. Pihlanto,. Food-derived bioactive peptides-opportunities for designing future foods. Curr. Pharm. Des. 2003, 9, 1297.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1297
    • Korhonen, H.1    Pihlanto, A.2
  • 57
    • 50649107220 scopus 로고    scopus 로고
    • Identification of food-derived bioactive peptides in blood and other biological samples
    • K. Sato, K. Iwai, M. Aito-Inoue,. Identification of food-derived bioactive peptides in blood and other biological samples. J. AOAC Int. 2008, 91, 995.
    • (2008) J. AOAC Int. , vol.91 , pp. 995
    • Sato, K.1    Iwai, K.2    Aito-Inoue, M.3
  • 58
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • K. Erdmann, B. W. Cheung, H. Schroder,. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J. Nutr. Biochem. 2008, 19, 643.
    • (2008) J. Nutr. Biochem. , vol.19 , pp. 643
    • Erdmann, K.1    Cheung, B.W.2    Schroder, H.3
  • 59
    • 0028922504 scopus 로고
    • Characterization of an antithrombotic peptide from kappa-casein in newborn plasma after milk ingestion
    • B. Chabance, P. Jolles, C. Izquierdo, E. Mazoyer, C. Francoual, L. Drouet, A. M. Fiat,. Characterization of an antithrombotic peptide from kappa-casein in newborn plasma after milk ingestion. Br. J. Nutr. 1995, 73, 583.
    • (1995) Br. J. Nutr. , vol.73 , pp. 583
    • Chabance, B.1    Jolles, P.2    Izquierdo, C.3    Mazoyer, E.4    Francoual, C.5    Drouet, L.6    Fiat, A.M.7
  • 60
    • 84860195220 scopus 로고    scopus 로고
    • Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk
    • K. Hinz, P. M. O'Connor, T. Huppertz, R. P. Ross, A. L. Kelly,. Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk. J. Dairy Res. 2012, 79, 185.
    • (2012) J. Dairy Res. , vol.79 , pp. 185
    • Hinz, K.1    O'Connor, P.M.2    Huppertz, T.3    Ross, R.P.4    Kelly, A.L.5
  • 61
    • 33947097920 scopus 로고    scopus 로고
    • Milk peptides and blood pressure
    • T. Jauhiainen, R. Korpela,. Milk peptides and blood pressure. J. Nutr. 2007, 137, 825S.
    • (2007) J. Nutr. , vol.137
    • Jauhiainen, T.1    Korpela, R.2
  • 63
    • 34248366062 scopus 로고    scopus 로고
    • Putting microbes to work: Dairy fermentation, cell factories and bioactive peptides. Part I: Overview
    • M. Hayes, R. P. Ross, G. F. Fitzgerald, C. Stanton,. Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview. Biotechnol. J. 2007, 2, 426.
    • (2007) Biotechnol. J. , vol.2 , pp. 426
    • Hayes, M.1    Ross, R.P.2    Fitzgerald, G.F.3    Stanton, C.4
  • 64
    • 0032077925 scopus 로고    scopus 로고
    • Sequence analysis of Camelus dromedarius milk caseins
    • S. Kappeler, Z. Farah, Z. Puhan,. Sequence analysis of Camelus dromedarius milk caseins. J. Dairy Res. 1998, 65, 209.
    • (1998) J. Dairy Res. , vol.65 , pp. 209
    • Kappeler, S.1    Farah, Z.2    Puhan, Z.3


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