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Volumn 16, Issue 7, 2016, Pages 1059-1068

Preventing N- and O-formylation of proteins when incubated in concentrated formic acid

Author keywords

Formic acid; N formylation; O formylation; Protein modifications; Protein solubilization; Technology

Indexed keywords

ESCHERICHIA COLI PROTEIN; FORMIC ACID; LYSINE; PEPTIDE DERIVATIVE; SERINE; THREONINE; FORMIC ACID DERIVATIVE; HISTONE; PEPTIDE FRAGMENT;

EID: 84960436973     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201500366     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 34250843131 scopus 로고    scopus 로고
    • Study on the structure and properties of wool keratin regenerated from formic acid
    • Aluigi, A., Zoccola, M., Vineis, C., Tonin, C. et al., Study on the structure and properties of wool keratin regenerated from formic acid. Int. J. Biol. Macromol. 2007, 41, 266-273.
    • (2007) Int. J. Biol. Macromol. , vol.41 , pp. 266-273
    • Aluigi, A.1    Zoccola, M.2    Vineis, C.3    Tonin, C.4
  • 2
    • 0242409681 scopus 로고    scopus 로고
    • The role of formic acid in solution stability and crystallization of silk protein polymer
    • Um, I. C., Kweon, H. Y., Lee, K. G., Park, Y. H., The role of formic acid in solution stability and crystallization of silk protein polymer. Int. J. Biol. Macromol. 2003, 33, 203-213.
    • (2003) Int. J. Biol. Macromol. , vol.33 , pp. 203-213
    • Um, I.C.1    Kweon, H.Y.2    Lee, K.G.3    Park, Y.H.4
  • 3
    • 84914377236 scopus 로고
    • The oxidative conversion of casein into protein free of methionine
    • Toennies, G., The oxidative conversion of casein into protein free of methionine. J. Biol. Chem. 1942, 145, 667-670.
    • (1942) J. Biol. Chem. , vol.145 , pp. 667-670
    • Toennies, G.1
  • 4
    • 38349032044 scopus 로고
    • The action of organic acids on some fibrous proteins: the oxidation of wool keratin
    • Blackburn, S., Lowther, A. G., The action of organic acids on some fibrous proteins: the oxidation of wool keratin. Biochem. J. 1951, 49, 554-559.
    • (1951) Biochem. J. , vol.49 , pp. 554-559
    • Blackburn, S.1    Lowther, A.G.2
  • 5
    • 0344388971 scopus 로고
    • Solubilization and fractionation of wheat flour proteins insoluble in dilute acetic acid
    • Inamine, E. S., Noble, E. G., Mecham, D. K., Solubilization and fractionation of wheat flour proteins insoluble in dilute acetic acid. Cereal Chem. 1967, 44, 143-151.
    • (1967) Cereal Chem , vol.44 , pp. 143-151
    • Inamine, E.S.1    Noble, E.G.2    Mecham, D.K.3
  • 6
    • 0016212987 scopus 로고
    • The dissolution of bovine and chicken bone collagens in concentrated formic acid
    • Eyre, D. R., Glimcher, M. J., The dissolution of bovine and chicken bone collagens in concentrated formic acid. Calcif. Tissue Res. 1974, 15, 125-132.
    • (1974) Calcif. Tissue Res. , vol.15 , pp. 125-132
    • Eyre, D.R.1    Glimcher, M.J.2
  • 7
    • 0025371975 scopus 로고
    • Alzheimer's beta-amyloid protein is covalently modified when dissolved in formic acid
    • Klunk, W. E., Pettegrew, J. W., Alzheimer's beta-amyloid protein is covalently modified when dissolved in formic acid. J. Neurochem. 1990, 62, 2050-2056.
    • (1990) J. Neurochem. , vol.62 , pp. 2050-2056
    • Klunk, W.E.1    Pettegrew, J.W.2
  • 8
    • 0034703634 scopus 로고    scopus 로고
    • Formic acid dissolves aggregates of an N-terminal huntingtin fragment containing an expanded polyglutamine tract: applying to quantification of protein components of the aggregates
    • Hazeki, N., Tukamoto, T., Goto, J., Kanazawa, I., Formic acid dissolves aggregates of an N-terminal huntingtin fragment containing an expanded polyglutamine tract: applying to quantification of protein components of the aggregates. Biochem. Biophys. Res. Commun. 2000, 277, 386-393.
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 386-393
    • Hazeki, N.1    Tukamoto, T.2    Goto, J.3    Kanazawa, I.4
  • 9
    • 0013805993 scopus 로고
    • Comparison of b-galactosidased from normal (i-o+z+) and Operator Constitutive (i-ocz+) strains of E. coli
    • Steers, E. Jr., Craven, G. R., Anfinsen, C. B., Comparison of b-galactosidased from normal (i-o+z+) and Operator Constitutive (i-ocz+) strains of E. coli. Biochemistry 1965, 54, 1174-1181.
    • (1965) Biochemistry , vol.54 , pp. 1174-1181
    • Steers, E.1    Craven, G.R.2    Anfinsen, C.B.3
  • 10
    • 0014548741 scopus 로고
    • Cleavage of bacterial flagellin with cyanogen bromide: chemical and physical properties of the protein fragments
    • Parish, C. R., Ada, G. L., Cleavage of bacterial flagellin with cyanogen bromide: chemical and physical properties of the protein fragments. Biochem. J. 1969, 113, 489-499.
    • (1969) Biochem. J. , vol.113 , pp. 489-499
    • Parish, C.R.1    Ada, G.L.2
  • 11
    • 0001067208 scopus 로고
    • Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide
    • Gross, E., Witkop, B., Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. J. Am. Chem. Soc. 1961, 83, 1510-1511.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 1510-1511
    • Gross, E.1    Witkop, B.2
  • 12
    • 0020014653 scopus 로고
    • Oxidation of methionine to methionine sulfoxide as a side reaction of cyanogen bromide cleavage
    • Joppich-Kuhn, R., Corkill, J. A., Giese, R. W., Oxidation of methionine to methionine sulfoxide as a side reaction of cyanogen bromide cleavage. Anal. Biochem. 1982, 119, 73-77.
    • (1982) Anal. Biochem. , vol.119 , pp. 73-77
    • Joppich-Kuhn, R.1    Corkill, J.A.2    Giese, R.W.3
  • 13
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins - theory and application
    • Speers, A. E., Wu, C. C., Proteomics of integral membrane proteins - theory and application. Chem. Rev. 2007, 107, 3687-3714.
    • (2007) Chem. Rev. , vol.107 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 14
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge, J. P., Gundersen, C. B., Faull, K. F., Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins. Protein Sci. 1998, 7, 1423-1430.
    • (1998) Protein Sci , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 15
    • 0020263340 scopus 로고
    • Reversed-phase high-performance liquid chromatography of virus proteins and other large hydrophobic proteins in formic acid containing solvents
    • Heukeshoven, J., Dernick, R., Reversed-phase high-performance liquid chromatography of virus proteins and other large hydrophobic proteins in formic acid containing solvents. J. Chromatogr. A 1982, 252, 241-254.
    • (1982) J. Chromatogr. A , vol.252 , pp. 241-254
    • Heukeshoven, J.1    Dernick, R.2
  • 16
    • 77957010574 scopus 로고
    • Cleavage at aspartic acid
    • Schultz, J., Cleavage at aspartic acid. Methods Enzymol. 1967, 11, 255-263.
    • (1967) Methods Enzymol , vol.11 , pp. 255-263
    • Schultz, J.1
  • 17
    • 0035891161 scopus 로고    scopus 로고
    • Chemical cleavage at aspartyl residues for protein identification
    • Li, A., Sowder, R. C., Henderson, L. E., Moore, S. P. et al., Chemical cleavage at aspartyl residues for protein identification. Anal. Chem. 2001, 73, 5395-5402.
    • (2001) Anal. Chem. , vol.73 , pp. 5395-5402
    • Li, A.1    Sowder, R.C.2    Henderson, L.E.3    Moore, S.P.4
  • 18
    • 78650769163 scopus 로고    scopus 로고
    • Rapid online non-enzymatic protein digestion combining microwave heating hydrolysis and electrochemical
    • Basile, F., Hauser, N., Rapid online non-enzymatic protein digestion combining microwave heating hydrolysis and electrochemical. Anal. Chem. 2012, 83, 359-367.
    • (2012) Anal. Chem. , vol.83 , pp. 359-367
    • Basile, F.1    Hauser, N.2
  • 19
    • 5044222901 scopus 로고    scopus 로고
    • Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis
    • Zhong, H., Zhang, Y., Wen, Z., Li, L., Protein sequencing by mass analysis of polypeptide ladders after controlled protein hydrolysis. Nat. Biotechnol. 2004, 22, 1291-1296.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1291-1296
    • Zhong, H.1    Zhang, Y.2    Wen, Z.3    Li, L.4
  • 20
    • 77951839609 scopus 로고    scopus 로고
    • Post-translational Modifications of Integral Membrane Proteins Resolved by Top-down Fourier Transform Mass Spectrometry with Collisionally Activated Dissociation
    • Ryan, C. M., Souda, P., Bassilian, S., Ujwal, R. et al., Post-translational Modifications of Integral Membrane Proteins Resolved by Top-down Fourier Transform Mass Spectrometry with Collisionally Activated Dissociation. Mol. Cell. Proteomics 2010, 9, 791-803.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 791-803
    • Ryan, C.M.1    Souda, P.2    Bassilian, S.3    Ujwal, R.4
  • 21
    • 33846985931 scopus 로고
    • Reaction of anhydrous formic acid with proteins
    • Narita, K., Reaction of anhydrous formic acid with proteins. J. Am. Chem. Soc. 1959, 81, 1751-1756
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 1751-1756
    • Narita, K.1
  • 22
    • 33846961769 scopus 로고
    • Action of anhydrous formic acid on peptides and proteins
    • Kienhuis, H., Blasse, G., Matze, J., Action of anhydrous formic acid on peptides and proteins. Nature 1959, 184, 2015-2016.
    • (1959) Nature , vol.184 , pp. 2015-2016
    • Kienhuis, H.1    Blasse, G.2    Matze, J.3
  • 23
    • 0028155882 scopus 로고
    • NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein
    • Klunk, W. E., Xu, C.-J., Pettegrew, J. W., NMR identification of the formic acid-modified residue in Alzheimer's amyloid protein. J. Neurochem. 1994, 62, 349-354.
    • (1994) J. Neurochem. , vol.62 , pp. 349-354
    • Klunk, W.E.1    Xu, C.-J.2    Pettegrew, J.W.3
  • 24
    • 0025356855 scopus 로고
    • Formylated peptides from cyanogen bromide digests identified by fast atom bombardment mass spectrometry
    • Goodlett, D. R., Armstrong, F. B., Creech, R. J., van Breemen, R. B., Formylated peptides from cyanogen bromide digests identified by fast atom bombardment mass spectrometry. Anal. Biochem. 1990, 186, 116-120.
    • (1990) Anal. Biochem. , vol.186 , pp. 116-120
    • Goodlett, D.R.1    Armstrong, F.B.2    Creech, R.J.3    van Breemen, R.B.4
  • 25
    • 84921794624 scopus 로고    scopus 로고
    • Trifluoroethanol-containing RP-HPLC mobile phases for the separation of transmembrane peptides human glycophorin-A, integrin alpha-1, and p24: analysis and prevention of potential side reactions due to formic acid
    • Hara, T., Huang, Y., Ito, A., Kawakami, T. et al., Trifluoroethanol-containing RP-HPLC mobile phases for the separation of transmembrane peptides human glycophorin-A, integrin alpha-1, and p24: analysis and prevention of potential side reactions due to formic acid. J. Pept. Sci. 2015, 21, 61-70.
    • (2015) J. Pept. Sci. , vol.21 , pp. 61-70
    • Hara, T.1    Huang, Y.2    Ito, A.3    Kawakami, T.4
  • 26
  • 27
    • 79956328671 scopus 로고    scopus 로고
    • An efficient, catalyst- and solvent-free N-formylation of aromatic and aliphatic amines
    • Dhake, K. P., Tambade, P. J., Singhal, R. S., Bhanage, B. M., An efficient, catalyst- and solvent-free N-formylation of aromatic and aliphatic amines. Green Chem. Lett. Rev. 2011, 4, 151-157.
    • (2011) Green Chem. Lett. Rev. , vol.4 , pp. 151-157
    • Dhake, K.P.1    Tambade, P.J.2    Singhal, R.S.3    Bhanage, B.M.4
  • 28
    • 77954192559 scopus 로고    scopus 로고
    • Amberlite IR-120: a reusable catalyst for N-formylation of amines with formic acid using microwaves
    • Muthukur Bhojegowd, M. R., Nizam, A., Pasha, M. A., Amberlite IR-120: a reusable catalyst for N-formylation of amines with formic acid using microwaves. Chinese J. Catal. 2010, 31, 518-520.
    • (2010) Chinese J. Catal. , vol.31 , pp. 518-520
    • Muthukur Bhojegowd, M.R.1    Nizam, A.2    Pasha, M.A.3
  • 29
    • 0013967817 scopus 로고
    • Initiation of protein synthesis, I. Effect of formylation of methionyl-tRNA on codon recognition
    • Philip, L., Bursztyn, H., Initiation of protein synthesis, I. Effect of formylation of methionyl-tRNA on codon recognition. Proc. Natl. Acad. Sci. U S A 1966, 56, 1579-1585.
    • (1966) Proc. Natl. Acad. Sci. U S A , vol.56 , pp. 1579-1585
    • Philip, L.1    Bursztyn, H.2
  • 30
    • 33646042375 scopus 로고    scopus 로고
    • Ligand recognition and activation of formyl peptide receptors in neutrophils
    • Fu, H., Karlsson, J., Bylund, J., Movitz, C. et al., Ligand recognition and activation of formyl peptide receptors in neutrophils. J. Leukoc. Biol. 2006, 79, 247-256.
    • (2006) J. Leukoc. Biol. , vol.79 , pp. 247-256
    • Fu, H.1    Karlsson, J.2    Bylund, J.3    Movitz, C.4
  • 31
    • 33846113751 scopus 로고    scopus 로고
    • N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage
    • Jiang, T., Zhou, X., Taghizadeh, K., Dong, M., Dedon, P. C., N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage. Proc. Natl. Acad. Sci. U S A 2007, 104, 60-65.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 60-65
    • Jiang, T.1    Zhou, X.2    Taghizadeh, K.3    Dong, M.4    Dedon, P.C.5
  • 32
    • 39149121854 scopus 로고    scopus 로고
    • ε-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
    • ε-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function. Nucleic Acids Res. 2008, 36, 570-577.
    • (2008) Nucleic Acids Res , vol.36 , pp. 570-577
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 33
    • 84923101475 scopus 로고    scopus 로고
    • Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair
    • Sone, K., Piao, L., Nakakido, M., Ueda, K. et al., Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair. Nat. Commun. 2014, 5, 5691.
    • (2014) Nat. Commun. , vol.5 , pp. 5691
    • Sone, K.1    Piao, L.2    Nakakido, M.3    Ueda, K.4
  • 34
    • 0035370439 scopus 로고    scopus 로고
    • Histone methylation versus histone acetylation: new insights into epigenetic regulation
    • Rice, J. C., Allis, C. D., Histone methylation versus histone acetylation: new insights into epigenetic regulation. Curr. Opin. Cell Biol. 2001, 13, 263-273.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 263-273
    • Rice, J.C.1    Allis, C.D.2
  • 35
    • 84925285779 scopus 로고    scopus 로고
    • Non-histone protein methylation as a regulator of cellular signalling and function
    • Biggar, K. K., Li, S. S.-C., Non-histone protein methylation as a regulator of cellular signalling and function. Nat. Rev. Mol. Cell Biol. 2014, 16, 5-17.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 5-17
    • Biggar, K.K.1    Li, S.S.-C.2
  • 37
    • 0029093338 scopus 로고
    • High-performance liquid chromatographic purification of extremely hydrophobic peptides: transmembrane segments
    • Bollhagen, R., Schmiedberger, M., Grell, E., High-performance liquid chromatographic purification of extremely hydrophobic peptides: transmembrane segments. J. Chromatogr. A 1995, 711, 181-186.
    • (1995) J. Chromatogr. A , vol.711 , pp. 181-186
    • Bollhagen, R.1    Schmiedberger, M.2    Grell, E.3
  • 38
    • 84915781391 scopus 로고    scopus 로고
    • Resolubilization of precipitated intact membrane proteins with cold formic acid for analysis by mass spectrometry
    • Doucette, A. A., Vieira, D. B., Orton, D. J., Wall, M. J., Resolubilization of precipitated intact membrane proteins with cold formic acid for analysis by mass spectrometry. J. Proteome Res. 2014, 13, 6001-6012.
    • (2014) J. Proteome Res. , vol.13 , pp. 6001-6012
    • Doucette, A.A.1    Vieira, D.B.2    Orton, D.J.3    Wall, M.J.4
  • 39
    • 84915743758 scopus 로고    scopus 로고
    • The QIAGEN guide to good microbiological practice. Part III: growth of E. coli cultures
    • The QIAGEN guide to good microbiological practice. Part III: growth of E. coli cultures. QIAGEN News 1999, 1, 17-19.
    • (1999) QIAGEN News , vol.1 , pp. 17-19
  • 40
    • 84874579170 scopus 로고    scopus 로고
    • A universal, high recovery assay for protein quantitation through temperature programmed liquid chromatography (TPLC)
    • Orton, D.J., Doucette, A. A., A universal, high recovery assay for protein quantitation through temperature programmed liquid chromatography (TPLC). J. Chromatogr. B 2013, 921-922, 75-80.
    • (2013) J. Chromatogr. B , vol.921-922 , pp. 75-80
    • Orton, D.J.1    Doucette, A.A.2
  • 41
    • 84890092602 scopus 로고    scopus 로고
    • Dual LC-MS platform for high-throughput proteome analysis
    • Orton, D. J., Wall, M. J., Doucette, A. A., Dual LC-MS platform for high-throughput proteome analysis. J. Proteome Res. 2013, 12, 5963-5970.
    • (2013) J. Proteome Res. , vol.12 , pp. 5963-5970
    • Orton, D.J.1    Wall, M.J.2    Doucette, A.A.3
  • 42
    • 36248957157 scopus 로고    scopus 로고
    • Application of the O-N intramolecular acyl migration reaction in medicinal chemistry
    • Skwarczynski, M., Kiso, Y., Application of the O-N intramolecular acyl migration reaction in medicinal chemistry. Curr. Med. Chem. 2007, 14, 2813-2823.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2813-2823
    • Skwarczynski, M.1    Kiso, Y.2
  • 43
  • 44
    • 84962089232 scopus 로고    scopus 로고
    • 92nd ed. Haynes W. M. (Ed.), CRC Press, Boca Raton, FL.
    • CRC Handbook of Chemistry & Physics, 92nd ed. in: Haynes W. M. (Ed.), CRC Press, Boca Raton, FL 2011, pp. 5-129.
    • (2011) CRC Handbook of Chemistry & Physics , pp. 5-129


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