메뉴 건너뛰기




Volumn 1794, Issue 4, 2009, Pages 698-708

Resistance of bromelain to SDS binding

Author keywords

Bromelain; Isothermal calorimetry; Partial inhibition; Protein stability; Resistance to SDS

Indexed keywords

BROMELAIN; DEOXYRIBONUCLEASE; PYRENE; RIBONUCLEASE;

EID: 61849108751     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.12.019     Document Type: Article
Times cited : (32)

References (47)
  • 1
    • 17644370014 scopus 로고    scopus 로고
    • Polymer-surfactant and protein-surfactant interactions
    • La Mesa C. Polymer-surfactant and protein-surfactant interactions. J. Coll. Int. Sci. 286 (2005) 148-157
    • (2005) J. Coll. Int. Sci. , vol.286 , pp. 148-157
    • La Mesa, C.1
  • 2
    • 0001285423 scopus 로고
    • Binding of n-alkyl sulphates to lysozyme in aqueous solution
    • Jones M.N., and Manley P. Binding of n-alkyl sulphates to lysozyme in aqueous solution. J. Chem. Soc., Faraday Trans. 75 (1979) 1736-1744
    • (1979) J. Chem. Soc., Faraday Trans. , vol.75 , pp. 1736-1744
    • Jones, M.N.1    Manley, P.2
  • 3
    • 0001684352 scopus 로고
    • Surfactant interactions with biomembranes and proteins
    • Jones M.N. Surfactant interactions with biomembranes and proteins. Chem. Soc. Rev. 21 (1992) 127-136
    • (1992) Chem. Soc. Rev. , vol.21 , pp. 127-136
    • Jones, M.N.1
  • 4
    • 0014063229 scopus 로고
    • The binding of diverse detergent anions to bovine serum albumin
    • Reynolds J.A., Herbert S., Polet H., and Steinhardt J. The binding of diverse detergent anions to bovine serum albumin. Biochemistry 6 (1967) 937-943
    • (1967) Biochemistry , vol.6 , pp. 937-943
    • Reynolds, J.A.1    Herbert, S.2    Polet, H.3    Steinhardt, J.4
  • 5
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius A., and Simons K. Solubilization of membranes by detergents. Biochim. Biophys. Acta 415 (1975) 29-79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 6
    • 0032871869 scopus 로고    scopus 로고
    • A comparative study of the unfolding of the endoglucanase Ce145 from Humicola insolens in denaturant and surfactant
    • Otzen D.E., Christiansen L., and Schülein M. A comparative study of the unfolding of the endoglucanase Ce145 from Humicola insolens in denaturant and surfactant. Protein Sci. 8 (1999) 1878-1887
    • (1999) Protein Sci. , vol.8 , pp. 1878-1887
    • Otzen, D.E.1    Christiansen, L.2    Schülein, M.3
  • 7
    • 33644759714 scopus 로고    scopus 로고
    • Peracetylated bovine carbonic anhydrase (BCA-Ac18) is kinetically more stable than native BCA to sodium dodecyl sulphate
    • Gitlin I., Gudiksen K.L., and Whitesides G.M. Peracetylated bovine carbonic anhydrase (BCA-Ac18) is kinetically more stable than native BCA to sodium dodecyl sulphate. J. Phys. Chem., B. 110 (2006) 2372-2377
    • (2006) J. Phys. Chem., B. , vol.110 , pp. 2372-2377
    • Gitlin, I.1    Gudiksen, K.L.2    Whitesides, G.M.3
  • 8
    • 0016221553 scopus 로고
    • Activation of a-amylase by protein and detergent
    • O'Donnell M.D., and McGeeney K.F. Activation of a-amylase by protein and detergent. Enzyme 18 (1972) 356-367
    • (1972) Enzyme , vol.18 , pp. 356-367
    • O'Donnell, M.D.1    McGeeney, K.F.2
  • 9
    • 0020189601 scopus 로고
    • Effect of solvents on the catalytic activity of firefly luciferase
    • Kricka L.J., and De Luca M. Effect of solvents on the catalytic activity of firefly luciferase. Arch. Biochem. Biophys. 217 (1982) 674-681
    • (1982) Arch. Biochem. Biophys. , vol.217 , pp. 674-681
    • Kricka, L.J.1    De Luca, M.2
  • 10
    • 0022239697 scopus 로고
    • Charged detergents enhance the activity of phospholipase C (Bacillus cereus) towards micellar short-chain phosphatidylcholine
    • El-Sayed M.Y., and Roberts M.F. Charged detergents enhance the activity of phospholipase C (Bacillus cereus) towards micellar short-chain phosphatidylcholine. Biochim. Biophys. Acta 831 (1985) 133-141
    • (1985) Biochim. Biophys. Acta , vol.831 , pp. 133-141
    • El-Sayed, M.Y.1    Roberts, M.F.2
  • 11
    • 0018712435 scopus 로고
    • Kinetic changes following modification of rat liver alcohol dehydrogenase by deoxycholate
    • Hanozet G.M., Simonetta M., Barisio D., and Guerritore A. Kinetic changes following modification of rat liver alcohol dehydrogenase by deoxycholate. Arch. Biochem. Biophys. 196 (1979) 46-53
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 46-53
    • Hanozet, G.M.1    Simonetta, M.2    Barisio, D.3    Guerritore, A.4
  • 12
    • 0003074147 scopus 로고
    • Proteinases
    • Fogarty W.M. (Ed), Applied Science, New York
    • Ward O.P. Proteinases. In: Fogarty W.M. (Ed). Microbial Enzymes and Biotechnology (1983), Applied Science, New York 251-305
    • (1983) Microbial Enzymes and Biotechnology , pp. 251-305
    • Ward, O.P.1
  • 13
    • 0034843751 scopus 로고    scopus 로고
    • Bromelain: biochemistry, pharmacology and medical use
    • Maurer H.R. Bromelain: biochemistry, pharmacology and medical use. Cell. Mol. Life Sci. 58 (2001) 1234-1245
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1234-1245
    • Maurer, H.R.1
  • 14
    • 77957015497 scopus 로고
    • Plant proteolytic enzymes
    • Colowick S.P., and Kaplan N.O. (Eds), Academic Press Inc., New York
    • Greenberg D.M. Plant proteolytic enzymes. In: Colowick S.P., and Kaplan N.O. (Eds). Methods in Enzymology Vol. 1 (1955), Academic Press Inc., New York 54-64
    • (1955) Methods in Enzymology , vol.1 , pp. 54-64
    • Greenberg, D.M.1
  • 15
    • 0009597950 scopus 로고
    • Proteasas de Bromeliaceae. II. Separación, caracterización y fraccionamiento de una proteasa aislada de frutos de Bromelia hieronymi
    • Natalucci C.L., Priolo N.S., Buttazzoni M.S., and Caffini N.O. Proteasas de Bromeliaceae. II. Separación, caracterización y fraccionamiento de una proteasa aislada de frutos de Bromelia hieronymi. Mez. Acta Farm. Bonaerense 4 (1985) 93-98
    • (1985) Mez. Acta Farm. Bonaerense , vol.4 , pp. 93-98
    • Natalucci, C.L.1    Priolo, N.S.2    Buttazzoni, M.S.3    Caffini, N.O.4
  • 16
    • 61849150699 scopus 로고
    • Fractionation, purification, and some properties of proteolytic enzymes from stem bromelain
    • Minami Y., Doi E., and Hata T. Fractionation, purification, and some properties of proteolytic enzymes from stem bromelain. Agric. Biol. Chem. 35 (1971) 1419-1430
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1419-1430
    • Minami, Y.1    Doi, E.2    Hata, T.3
  • 18
    • 4444330121 scopus 로고    scopus 로고
    • Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward β-sheet structure
    • Manning M., and Colon W. Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward β-sheet structure. Biochemistry 43 (2004) 11248-11254
    • (2004) Biochemistry , vol.43 , pp. 11248-11254
    • Manning, M.1    Colon, W.2
  • 19
    • 77956999851 scopus 로고
    • Bromelain enzymes
    • Murachi T. Bromelain enzymes. Methods Enzymol. 19 (1970) 273-284
    • (1970) Methods Enzymol. , vol.19 , pp. 273-284
    • Murachi, T.1
  • 20
    • 0024551586 scopus 로고
    • Stem bromelain: amino acid sequence and implications for weak binding of cystatin
    • Ritonja A., Rowan A.D., Buttle D.J., Rawlings N.D., Turk V., and Barrett A.J. Stem bromelain: amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247 (1989) 419-424
    • (1989) FEBS Lett. , vol.247 , pp. 419-424
    • Ritonja, A.1    Rowan, A.D.2    Buttle, D.J.3    Rawlings, N.D.4    Turk, V.5    Barrett, A.J.6
  • 21
    • 0028672814 scopus 로고
    • Pineapple cysteine endopeptidaes
    • Rowan A.D., and Buttle D.J. Pineapple cysteine endopeptidaes. Methods Enzymol. 244 (1994) 555-568
    • (1994) Methods Enzymol. , vol.244 , pp. 555-568
    • Rowan, A.D.1    Buttle, D.J.2
  • 23
    • 0023657099 scopus 로고
    • A graphical method for determining inhibition parameters for partial and complete inhibitors
    • Yoshino M. A graphical method for determining inhibition parameters for partial and complete inhibitors. Biochem. J. 248 (1987) 815-820
    • (1987) Biochem. J. , vol.248 , pp. 815-820
    • Yoshino, M.1
  • 24
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chaćon P., Merelo J.J., and Moŕan F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chaćon, P.2    Merelo, J.J.3    Moŕan, F.4
  • 25
    • 0014718113 scopus 로고
    • Protein denaturation: theoretical models for the mechanism of denaturation
    • Anfinsen Jr. C.B., and Edsall J.T. (Eds), Academic Press Inc., New York
    • Tanford C. Protein denaturation: theoretical models for the mechanism of denaturation. In: Anfinsen Jr. C.B., and Edsall J.T. (Eds). Advances in Protein Chemistry (1970), Academic Press Inc., New York 2-95
    • (1970) Advances in Protein Chemistry , pp. 2-95
    • Tanford, C.1
  • 27
    • 0028287393 scopus 로고
    • Circular dichroism of stem bromelain: a third spectral class within the family of cysteine proteinases
    • Arroyo-Reyna A., Hernandez-Arana A., and Arregiun-Espinosa R. Circular dichroism of stem bromelain: a third spectral class within the family of cysteine proteinases. Biochem. J. 300 (1994) 107-110
    • (1994) Biochem. J. , vol.300 , pp. 107-110
    • Arroyo-Reyna, A.1    Hernandez-Arana, A.2    Arregiun-Espinosa, R.3
  • 28
    • 0019602362 scopus 로고
    • Pyrene fluorescence fine structure as a polarity probe of hydrophobic regions: behavior in model solvents
    • Glushko U., Thaler M.S.R., and Karp C.D. Pyrene fluorescence fine structure as a polarity probe of hydrophobic regions: behavior in model solvents. Arch. Biochem. Biophys. 210 (1981) 33-42
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 33-42
    • Glushko, U.1    Thaler, M.S.R.2    Karp, C.D.3
  • 29
    • 84985445694 scopus 로고
    • Solvent effects on the vibronic fine structure of pyrene fluorescence and empirical correlations with ET and Y values
    • Dong D.C., and Winnik M.A. Solvent effects on the vibronic fine structure of pyrene fluorescence and empirical correlations with ET and Y values. Photochem. Photobiol. 35 (1982) 17-21
    • (1982) Photochem. Photobiol. , vol.35 , pp. 17-21
    • Dong, D.C.1    Winnik, M.A.2
  • 30
    • 0022625326 scopus 로고
    • Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-1-naphthylamine
    • Brito R.M., and Vaz W.L. Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-1-naphthylamine. Anal. Biochem. 152 (1986) 250-255
    • (1986) Anal. Biochem. , vol.152 , pp. 250-255
    • Brito, R.M.1    Vaz, W.L.2
  • 31
    • 0034659669 scopus 로고    scopus 로고
    • Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin
    • Nielsen A.D., Borch K., and Westh P. Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin. Biochim. Biophys. Acta 1479 (2000) 321-331
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 321-331
    • Nielsen, A.D.1    Borch, K.2    Westh, P.3
  • 32
    • 18844380718 scopus 로고    scopus 로고
    • Interactions of Humicola insolens cutinase with an anionic surfactant studied by small-angle neutron scattering and isothermal titration calorimetry
    • Nielsen A.D., Arleth L., and Westh P. Interactions of Humicola insolens cutinase with an anionic surfactant studied by small-angle neutron scattering and isothermal titration calorimetry. Langmuir 21 (2005) 4299-4307
    • (2005) Langmuir , vol.21 , pp. 4299-4307
    • Nielsen, A.D.1    Arleth, L.2    Westh, P.3
  • 34
    • 0037240012 scopus 로고    scopus 로고
    • Interactions of bovine serum albumin with ionic surfactants in aqueous solutions
    • Kelley D., and McClements D.J. Interactions of bovine serum albumin with ionic surfactants in aqueous solutions. Food. Hydrocolloids. 17 (2003) 73-85
    • (2003) Food. Hydrocolloids. , vol.17 , pp. 73-85
    • Kelley, D.1    McClements, D.J.2
  • 35
    • 33751156138 scopus 로고
    • Thermodynamics of micelle formation as a function of temperature - a highsensitivity titration calorimetry study
    • Paula S., Sus W., Tuchtenhagen J., and Blume A. Thermodynamics of micelle formation as a function of temperature - a highsensitivity titration calorimetry study. J. Phys. Chem. 99 (1995) 11742-11751
    • (1995) J. Phys. Chem. , vol.99 , pp. 11742-11751
    • Paula, S.1    Sus, W.2    Tuchtenhagen, J.3    Blume, A.4
  • 36
    • 25144460975 scopus 로고    scopus 로고
    • Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant
    • Nielsen A.D., Arleth L., and Westh P. Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant. Biochim. Biophys. Acta 1752 (2005) 124-132
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 124-132
    • Nielsen, A.D.1    Arleth, L.2    Westh, P.3
  • 37
    • 0037008404 scopus 로고    scopus 로고
    • Studies on surfactant-biopolymer interaction: I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA)
    • Chatterjee A., Moulik S.P., Majhi P.R., and Sanyal S.K. Studies on surfactant-biopolymer interaction: I. Microcalorimetric investigation on the interaction of cetyltrimethylammonium bromide (CTAB) and sodium dodecylsulfate (SDS) with gelatin (Gn), lysozyme (Lz) and deoxyribonucleic acid (DNA). Biophys. Chem. 98 (2002) 313-327
    • (2002) Biophys. Chem. , vol.98 , pp. 313-327
    • Chatterjee, A.1    Moulik, S.P.2    Majhi, P.R.3    Sanyal, S.K.4
  • 38
    • 0001043064 scopus 로고
    • Proteins and sodium dodecyl sulfate: molecular weight determination on polyacrylamide gels and related structures
    • Neurath H., and Hill R.L. (Eds), Academic Press Inc., New York
    • Weber K., and Osborn M. Proteins and sodium dodecyl sulfate: molecular weight determination on polyacrylamide gels and related structures. In: Neurath H., and Hill R.L. (Eds). The Proteins. 3rd edn. Vol. 1 (1975), Academic Press Inc., New York 179-223
    • (1975) The Proteins. 3rd edn. , vol.1 , pp. 179-223
    • Weber, K.1    Osborn, M.2
  • 39
    • 0025268799 scopus 로고
    • The cysteine proteinases of pineapple plant
    • Rowan A.D., Buttle D.J., and Barrett A.J. The cysteine proteinases of pineapple plant. Biochem. J. 266 (1990) 869-875
    • (1990) Biochem. J. , vol.266 , pp. 869-875
    • Rowan, A.D.1    Buttle, D.J.2    Barrett, A.J.3
  • 40
    • 0035820418 scopus 로고    scopus 로고
    • Activation of enzymes for nonaqueous biocatalysis by denaturing concentrations of urea
    • Guo Y., and Clark D.S. Activation of enzymes for nonaqueous biocatalysis by denaturing concentrations of urea. Biochim. Biophys. Acta 1546 (2001) 406-411
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 406-411
    • Guo, Y.1    Clark, D.S.2
  • 42
    • 0017175473 scopus 로고
    • 1-acid glycoprotein, Bence Jones protein, carbonic anhydrase B, deoxyribonuclease, pepsinogen and plasminogen
    • 1-acid glycoprotein, Bence Jones protein, carbonic anhydrase B, deoxyribonuclease, pepsinogen and plasminogen. Biochim. Biophys. Acta 434 (1976) 58-68
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 58-68
    • Jirgensons, B.1
  • 43
    • 0030894087 scopus 로고    scopus 로고
    • Stability and activity of potato acid phosphatase in aqueous surfactant media
    • Lalitha J., and Mulimani V.H. Stability and activity of potato acid phosphatase in aqueous surfactant media. Biochem. Mol. Biol. Int. 41 (1997) 797-803
    • (1997) Biochem. Mol. Biol. Int. , vol.41 , pp. 797-803
    • Lalitha, J.1    Mulimani, V.H.2
  • 44
    • 0028807509 scopus 로고
    • Inactivation precedes overall molecular conformation changes during enzyme denaturation
    • Tsou C.-L. Inactivation precedes overall molecular conformation changes during enzyme denaturation. Biochim. Biophys. Acta 1253 (1995) 151-162
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 151-162
    • Tsou, C.-L.1
  • 45
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Wiliston S., Brandt J.F., and Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179 (1989) 131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Wiliston, S.2    Brandt, J.F.3    Lin, L.N.4
  • 46
    • 0036787578 scopus 로고    scopus 로고
    • Protein unfolding in detergents: effect of micelle structure, ionic strength, pH and temperature
    • Otzen D.E. Protein unfolding in detergents: effect of micelle structure, ionic strength, pH and temperature. Biophys. J. 83 (2002) 2219-2230
    • (2002) Biophys. J. , vol.83 , pp. 2219-2230
    • Otzen, D.E.1
  • 47
    • 0036307492 scopus 로고    scopus 로고
    • Burst-phase expansion of native protein prior to global unfolding in SDS
    • Otzen D.E., and Oliveberg M. Burst-phase expansion of native protein prior to global unfolding in SDS. J. Mol. Biol. 315 (2002) 1231-1240
    • (2002) J. Mol. Biol. , vol.315 , pp. 1231-1240
    • Otzen, D.E.1    Oliveberg, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.