메뉴 건너뛰기




Volumn 50, Issue 3, 2014, Pages 447-454

Interactions between proteins and humic substances affect protein identification by mass spectrometry

Author keywords

Humic substances; Mass spectrometry; Proteins in soil; Soil proteomics

Indexed keywords

ELECTROKINESIS; ENZYME ACTIVITY; HUMIC SUBSTANCE; MASS SPECTROMETRY; PROTEIN; PROTEOMICS; SOIL ANALYSIS; SOIL ORGANIC MATTER;

EID: 84897496489     PISSN: 01782762     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00374-013-0860-0     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M (2003) Mass spectrometry-based proteomics. Nature 13: 198-207.
    • (2003) Nature , vol.13 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 77957151118 scopus 로고
    • A review of recent work on soil organic matter
    • Bremner JM (1951) A review of recent work on soil organic matter. J Soil Sci 2: 67-82.
    • (1951) J Soil Sci , vol.2 , pp. 67-82
    • Bremner, J.M.1
  • 3
    • 0034120271 scopus 로고    scopus 로고
    • Interaction of catalase with montmorillonite homoionic to cations with different hydrophobicity: effect on bound enzyme activity
    • Calamai L, Lozzi I, Ristori GG, Fusi P, Stotzky G (2000) Interaction of catalase with montmorillonite homoionic to cations with different hydrophobicity: effect on bound enzyme activity. Soil Biol Biochem 32: 815-823.
    • (2000) Soil Biol Biochem , vol.32 , pp. 815-823
    • Calamai, L.1    Lozzi, I.2    Ristori, G.G.3    Fusi, P.4    Stotzky, G.5
  • 6
    • 0037090377 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry
    • Daniel JM, Friess SD, Rajagopalan S, Wendt S, Zenobi R (2002) Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry. Int J Mass Spectrom 216: 1-27.
    • (2002) Int J Mass Spectrom , vol.216 , pp. 1-27
    • Daniel, J.M.1    Friess, S.D.2    Rajagopalan, S.3    Wendt, S.4    Zenobi, R.5
  • 9
    • 79959263453 scopus 로고    scopus 로고
    • Structural analysis and binding domain of albumin complexes with natural dietary supplement humic acid
    • Ding F, Diao JX, Yang XL, Sun Y (2011) Structural analysis and binding domain of albumin complexes with natural dietary supplement humic acid. J Lumin 131: 2244-2251.
    • (2011) J Lumin , vol.131 , pp. 2244-2251
    • Ding, F.1    Diao, J.X.2    Yang, X.L.3    Sun, Y.4
  • 12
    • 0029251458 scopus 로고
    • Structures and stabilities of adsorbed proteins
    • Haynes CA, Norde WJ (1995) Structures and stabilities of adsorbed proteins. J Colloid Interface Sci 169: 313-328.
    • (1995) J Colloid Interface Sci , vol.169 , pp. 313-328
    • Haynes, C.A.1    Norde, W.J.2
  • 13
    • 26444451103 scopus 로고    scopus 로고
    • New evidence for covalent coupling of peptides to humic acids based on 2D NMR spectroscopy: a means for preservation
    • Hsu PH, Hatcher PG (2005) New evidence for covalent coupling of peptides to humic acids based on 2D NMR spectroscopy: a means for preservation. Geochim Cosmochim Acta 69: 4521-4533.
    • (2005) Geochim Cosmochim Acta , vol.69 , pp. 4521-4533
    • Hsu, P.H.1    Hatcher, P.G.2
  • 14
    • 63849104493 scopus 로고    scopus 로고
    • Environmental proteomics: a paradigm shift in characterizing microbial activities at the molecular level
    • Keller M, Hettich R (2009) Environmental proteomics: a paradigm shift in characterizing microbial activities at the molecular level. Microbiol Mol Biol Rev 73: 62-70.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 62-70
    • Keller, M.1    Hettich, R.2
  • 15
    • 38049060254 scopus 로고    scopus 로고
    • A proteomics strategy to discover β-glucosidases from Aspergillus fumigatus with two-dimensional page in-gel activity assay and tandem mass spectrometry
    • Kim KH, Brown KM, Harris PV, Langston JA, Cherry JR (2007) A proteomics strategy to discover β-glucosidases from Aspergillus fumigatus with two-dimensional page in-gel activity assay and tandem mass spectrometry. J Proteome Res 6: 4749-4757.
    • (2007) J Proteome Res , vol.6 , pp. 4749-4757
    • Kim, K.H.1    Brown, K.M.2    Harris, P.V.3    Langston, J.A.4    Cherry, J.R.5
  • 16
    • 33745943572 scopus 로고    scopus 로고
    • Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (membrane) protein complexes and supercomplexes
    • Krause F (2006) Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (membrane) protein complexes and supercomplexes. Electrophoresis 27: 2759-2781.
    • (2006) Electrophoresis , vol.27 , pp. 2759-2781
    • Krause, F.1
  • 17
    • 0020475449 scopus 로고
    • Simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RA (1982) Simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.A.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 15: 680-685.
    • (1970) Nature , vol.15 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 3042739098 scopus 로고    scopus 로고
    • Tool to visualize and evaluate data obtained by liquid chromatography-electrospray ionization-mass spectrometry
    • Li XJ, Pedrioli PA, Eng J, Martin D, Yi EC, Lee H, Aebersold RA (2004) Tool to visualize and evaluate data obtained by liquid chromatography-electrospray ionization-mass spectrometry. Anal Chem 76: 3856-3860.
    • (2004) Anal Chem , vol.76 , pp. 3856-3860
    • Li, X.J.1    Pedrioli, P.A.2    Eng, J.3    Martin, D.4    Yi, E.C.5    Lee, H.6    Aebersold, R.A.7
  • 20
    • 0010375449 scopus 로고
    • The role of carbohydrates in the free enzymes in soil
    • C. H. Fuschman (Ed.), London: Elsevier
    • Mayaudon J (1986) The role of carbohydrates in the free enzymes in soil. In: Fuschman CH (ed) Peat and water. Elsevier, London, pp 263-309.
    • (1986) Peat and Water , pp. 263-309
    • Mayaudon, J.1
  • 21
    • 55549109781 scopus 로고    scopus 로고
    • Role of stabilized enzymes in microbial ecology and enzyme extraction from soil with potential applications in nucleic acids and proteins in soils
    • In: Smalla K, Nannipieri P (eds). Soil Biology, Springer, Berlin
    • Nannipieri P (2006) Role of stabilized enzymes in microbial ecology and enzyme extraction from soil with potential applications in nucleic acids and proteins in soils. In: Smalla K, Nannipieri P (eds) Nucleic acids and proteins in soil. Soil Biology, Springer, Berlin, pp 75-94.
    • (2006) Nucleic acids and proteins in soil , pp. 75-94
    • Nannipieri, P.1
  • 24
    • 78649396817 scopus 로고    scopus 로고
    • Limitations of electrospray ionization in the analysis of a heterogeneous mixture of naturally occurring hydrophilic and hydrophobic compounds
    • Nebbioso A, Piccolo A, Spiteller M (2010) Limitations of electrospray ionization in the analysis of a heterogeneous mixture of naturally occurring hydrophilic and hydrophobic compounds. Rapid Commun Mass Spectrom 24: 3163-3170.
    • (2010) Rapid Commun Mass Spectrom , vol.24 , pp. 3163-3170
    • Nebbioso, A.1    Piccolo, A.2    Spiteller, M.3
  • 25
    • 0030532365 scopus 로고    scopus 로고
    • Driving forces for protein adsorption at solid surfaces
    • Norde W (1996) Driving forces for protein adsorption at solid surfaces. Macromol Symp 103: 5-18.
    • (1996) Macromol Symp , vol.103 , pp. 5-18
    • Norde, W.1
  • 26
    • 77951263539 scopus 로고    scopus 로고
    • Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown
    • Ogawa M, Nishio T, Minoura K, Uozumi T, Wada M, Hashimoto N, Kawachi R, Oku T (2006) Physical and kinetic properties of the family 3 beta-glucosidase from Aspergillus niger which is important for cellulose breakdown. J Appl Glycosci 53: 13-16.
    • (2006) J Appl Glycosci , vol.53 , pp. 13-16
    • Ogawa, M.1    Nishio, T.2    Minoura, K.3    Uozumi, T.4    Wada, M.5    Hashimoto, N.6    Kawachi, R.7    Oku, T.8
  • 27
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJC, Creasy DM, Cottrel JS (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrel, J.S.4
  • 28
    • 0035212659 scopus 로고    scopus 로고
    • The supramolecular structure of humic substances
    • Piccolo A (2001) The supramolecular structure of humic substances. Soil Sci 166: 810-832.
    • (2001) Soil Sci , vol.166 , pp. 810-832
    • Piccolo, A.1
  • 29
    • 0031795334 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry for the study of non-covalent complexes: an emerging technology
    • Pramanik BN, Bartner PL, Mirza UA, Liu YH, Ganguly AK (1998) Electrospray ionization mass spectrometry for the study of non-covalent complexes: an emerging technology. J Mass Spectrom 33: 911-920.
    • (1998) J Mass Spectrom , vol.33 , pp. 911-920
    • Pramanik, B.N.1    Bartner, P.L.2    Mirza, U.A.3    Liu, Y.H.4    Ganguly, A.K.5
  • 30
    • 84864632952 scopus 로고    scopus 로고
    • Covalent cross-linking within supramolecular peptide structures
    • Preston GW, Radford SE, Ashcroft AE, Wilson A (2012) Covalent cross-linking within supramolecular peptide structures. Anal Chem 84: 6790-6797.
    • (2012) Anal Chem , vol.84 , pp. 6790-6797
    • Preston, G.W.1    Radford, S.E.2    Ashcroft, A.E.3    Wilson, A.4
  • 31
    • 0026820432 scopus 로고
    • 31P NMR study of the adsorption of bovine serum albumin on montmorillonite using phosphate and the paramagnetic cation Mn2+: modification of conformation with pH
    • 31P NMR study of the adsorption of bovine serum albumin on montmorillonite using phosphate and the paramagnetic cation Mn2+: modification of conformation with pH. J Colloid Interface Sci 148: 343-352.
    • (1992) J Colloid Interface Sci , vol.148 , pp. 343-352
    • Quiquampoix, H.1    Ratcliffe, R.G.2
  • 32
    • 0036158672 scopus 로고    scopus 로고
    • Hydrolase activity during and after the chloroform fumigation of soils as affected by protease activity
    • Renella G, Landi L, Nannipieri P (2002) Hydrolase activity during and after the chloroform fumigation of soils as affected by protease activity. Soil Biol Biochem 34: 51-60.
    • (2002) Soil Biol Biochem , vol.34 , pp. 51-60
    • Renella, G.1    Landi, L.2    Nannipieri, P.3
  • 33
    • 85010063892 scopus 로고    scopus 로고
    • Soil proteomics
    • In: Nannipieri P, Pietramellara G, Renella G (eds). Horizon Scientific and Caister Academic, Norwich, in press
    • Renella G, Giagnoni L, Arenella M, Nannipieri P (2014) Soil proteomics. In: Nannipieri P, Pietramellara G, Renella G (eds) Omics in soil science. Horizon Scientific and Caister Academic, Norwich, in press.
    • (2014) Omics in soil science
    • Renella, G.1    Giagnoni, L.2    Arenella, M.3    Nannipieri, P.4
  • 34
    • 23144450894 scopus 로고    scopus 로고
    • Fate of prions in soil: trapped conformation of full-length ovine prion protein induced by adsorption on clays
    • Revault M, Quiquampoix H, Baron MH, Noinville S (2005) Fate of prions in soil: trapped conformation of full-length ovine prion protein induced by adsorption on clays. BBA-Gen Subj 1724: 367-374.
    • (2005) BBA-Gen Subj , vol.1724 , pp. 367-374
    • Revault, M.1    Quiquampoix, H.2    Baron, M.H.3    Noinville, S.4
  • 36
    • 33847537194 scopus 로고    scopus 로고
    • Organic matter characterization
    • D. L. Sparks, A. L. Page, P. A. Helmke, R. H. Loeppert, P. N. Soltanpour, M. A. Tabatabai, C. T. Johnston, and M. E. Summer (Eds.), Madison: American Society of Agronomy, Soil Science Society of America
    • Swift RG (1996) Organic matter characterization. In: Sparks DL, Page AL, Helmke PA, Loeppert RH, Soltanpour PN, Tabatabai MA, Johnston CT, Summer ME (eds) Methods of soil analysis. Part 3. Chemical methods. American Society of Agronomy, Soil Science Society of America, Madison, pp 1011-1069.
    • (1996) Methods of Soil Analysis. Part 3. Chemical Methods , pp. 1011-1069
    • Swift, R.G.1
  • 40
    • 79957788650 scopus 로고    scopus 로고
    • Comparative metaproteomic analysis on consecutively Rehmannia glutinosa-monocultured rhizosphere soil
    • Wu L, Wang H, Zhang Z, Lin R, Zhang Z, Lin W (2011) Comparative metaproteomic analysis on consecutively Rehmannia glutinosa-monocultured rhizosphere soil. Plos One 6: e20611.
    • (2011) Plos One , vol.6
    • Wu, L.1    Wang, H.2    Zhang, Z.3    Lin, R.4    Zhang, Z.5    Lin, W.6
  • 41
    • 0034233269 scopus 로고    scopus 로고
    • Encapsulation of protein in humic acid from a histosol as an explanation for the occurrence of organic nitrogen in soil and sediment
    • Zang X, van Heemst JDH, Dria KJ, Hatcher PG (2000) Encapsulation of protein in humic acid from a histosol as an explanation for the occurrence of organic nitrogen in soil and sediment. Org Geochem 31: 679-695.
    • (2000) Org Geochem , vol.31 , pp. 679-695
    • Zang, X.1    van Heemst, J.D.H.2    Dria, K.J.3    Hatcher, P.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.