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Volumn 81, Issue 5, 2003, Pages 327-333

Inactivation and conformational changes of creatine kinase at low concentrations of hexafluoroisopropanol solutions

Author keywords

Conformation; Creatine kinase; Hexafluoroisopropanol; Inactivation; Kinetics

Indexed keywords

BIOASSAY; CONFORMATIONS; ENZYMES; FLUORESCENCE;

EID: 0348134977     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o03-061     Document Type: Article
Times cited : (4)

References (24)
  • 1
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M.A., Chacon, P., Merelo, J.J., and Moran, F. 1993. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6: 383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 2
    • 0034167552 scopus 로고    scopus 로고
    • Effect of methanol on the activity and conformation of acid phosphatase from the prawn Penaeus penicillatus
    • Mosc.
    • Chen, Q.X., Zhang, R.Q., Xue, X.Z., Yang, D.Z., Chen, S.L., and Zhou, H.M. 2000. Effect of methanol on the activity and conformation of acid phosphatase from the prawn Penaeus penicillatus. Biochemistry (Mosc.), 65: 452-456.
    • (2000) Biochemistry , vol.65 , pp. 452-456
    • Chen, Q.X.1    Zhang, R.Q.2    Xue, X.Z.3    Yang, D.Z.4    Chen, S.L.5    Zhou, H.M.6
  • 3
    • 0031018220 scopus 로고    scopus 로고
    • Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: Evidence for a multiple-step process
    • Clottes, E., Leydier, C., Couthon, F., Marcillat, O., and Vial, C. 1997. Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: evidence for a multiple-step process. Biochim. Biophys. Acta, 1338: 37-46.
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 37-46
    • Clottes, E.1    Leydier, C.2    Couthon, F.3    Marcillat, O.4    Vial, C.5
  • 4
    • 0028829823 scopus 로고
    • Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea
    • Couthon, F., Clottes, E., Ebel, C., and Vial, C. 1995. Reversible dissociation and unfolding of dimeric creatine kinase isoenzyme MM in guanidine hydrochloride and urea. Eur. J. Biochem. 234: 160-170.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 160-170
    • Couthon, F.1    Clottes, E.2    Ebel, C.3    Vial, C.4
  • 5
    • 0033055898 scopus 로고    scopus 로고
    • Trifluoroethanol-induced conformational transitions of proteins: Insights gained from the differences between alpha-lactalbumin and ribonuclease A
    • Gast, K., Zirwer, D., Muller-Frohne, M., and Damaschun, G. 1999. Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A. Protein Sci. 8: 625-634.
    • (1999) Protein Sci. , vol.8 , pp. 625-634
    • Gast, K.1    Zirwer, D.2    Muller-Frohne, M.3    Damaschun, G.4
  • 6
    • 0029143228 scopus 로고
    • Multiple-state equilibrium unfolding guanidine kinase
    • Gross, M., Lustig, A., Wallimanm, T., and Furter, R. 1995. Multiple-state equilibrium unfolding guanidine kinase. Biochemistry, 34: 10 350-10 357.
    • (1995) Biochemistry , vol.34 , pp. 10350-10357
    • Gross, M.1    Lustig, A.2    Wallimanm, T.3    Furter, R.4
  • 7
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
    • Hamada, D., and Goto, Y. 1997. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. J. Mol. Biol. 269: 479-487.
    • (1997) J. Mol. Biol. , vol.269 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 8
    • 0031042309 scopus 로고    scopus 로고
    • Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol
    • Hirota, N., Mizuno, K., and Goto, Y. 1997. Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6: 416-421.
    • (1997) Protein Sci. , vol.6 , pp. 416-421
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 9
    • 0035830763 scopus 로고    scopus 로고
    • Reactivation and refolding of rabbit muscle creatine kinase denatured in 2,2,2-trifluoroethanol solutions
    • Huang, K., Park, Y.D., Cao, Z.F., and Zhou, H.M. 2001. Reactivation and refolding of rabbit muscle creatine kinase denatured in 2,2,2-trifluoroethanol solutions. Biochim. Biophys. Acta, 1545: 305-313.
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 305-313
    • Huang, K.1    Park, Y.D.2    Cao, Z.F.3    Zhou, H.M.4
  • 10
    • 0034025219 scopus 로고    scopus 로고
    • Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c
    • Konno, T., Twashita, J., and Nagayama, K. 2000. Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c. Protein Sci. 9: 564-569.
    • (2000) Protein Sci. , vol.9 , pp. 564-569
    • Konno, T.1    Twashita, J.2    Nagayama, K.3
  • 11
    • 0029620988 scopus 로고
    • Nonideality of water-hexafluoropropanol mixtures as studied by x-ray small angle scattering
    • Kuprin, S., Graslund, A., Ehrenberg, A., and Koch, M.H. 1995. Nonideality of water-hexafluoropropanol mixtures as studied by x-ray small angle scattering. Biochem. Biophys. Res. Commun. 217: 1151-1156.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1151-1156
    • Kuprin, S.1    Graslund, A.2    Ehrenberg, A.3    Koch, M.H.4
  • 12
    • 0034493728 scopus 로고    scopus 로고
    • Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide side chains
    • Reiersen, H., and Rees, A.R. 2000. Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide side chains. Protein Eng. 13: 739-743.
    • (2000) Protein Eng. , vol.13 , pp. 739-743
    • Reiersen, H.1    Rees, A.R.2
  • 13
    • 0037126023 scopus 로고    scopus 로고
    • Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study
    • Roccatano, D., Colombo, G., Fioroni, M., and Mark, A.E. 2002. Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study. Proc. Natl. Acad. Sci. U.S.A. 99: 12 179-12 184.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12179-12184
    • Roccatano, D.1    Colombo, G.2    Fioroni, M.3    Mark, A.E.4
  • 14
    • 0030593499 scopus 로고    scopus 로고
    • Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat
    • Schonbrunner, N., Wey, J., Engels, J., Gerog, H., and Kiefhaber, T. 1996. Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat. J. Mol. Biol. 260: 432-445.
    • (1996) J. Mol. Biol. , vol.260 , pp. 432-445
    • Schonbrunner, N.1    Wey, J.2    Engels, J.3    Gerog, H.4    Kiefhaber, T.5
  • 15
    • 0023739543 scopus 로고
    • Kinetics of substrate reaction during irreversible modification of enzyme activity
    • Tsou, C.L. 1988. Kinetics of substrate reaction during irreversible modification of enzyme activity. Adv. Enzymol. Related Areas Mol. Biol. 61: 381-436.
    • (1988) Adv. Enzymol. Related Areas Mol. Biol. , vol.61 , pp. 381-436
    • Tsou, C.L.1
  • 16
    • 0027496217 scopus 로고
    • Conformational flexibility of enzyme active sites
    • Washington, D.C.
    • Tsou, C.L. 1993. Conformational flexibility of enzyme active sites. Science (Washington, D.C.), 262: 380-381.
    • (1993) Science , vol.262 , pp. 380-381
    • Tsou, C.L.1
  • 17
    • 0023647288 scopus 로고
    • Kinetics of substrate reaction during irreversible modification of enzyme activity for enzymes involving two substrates
    • Wang, Z.X., and Tsou, C.L. 1987. Kinetics of substrate reaction during irreversible modification of enzyme activity for enzymes involving two substrates. J. Theor. Biol. 127: 253-270.
    • (1987) J. Theor. Biol. , vol.127 , pp. 253-270
    • Wang, Z.X.1    Tsou, C.L.2
  • 18
    • 0023801377 scopus 로고
    • Kinetics of inactivation of creatine kinase during modification of its thiol groups
    • Wang, Z.X., Preiss, B., and Tsou, C.L. 1988. Kinetics of inactivation of creatine kinase during modification of its thiol groups. Biochemistry, 27: 5095-5100.
    • (1988) Biochemistry , vol.27 , pp. 5095-5100
    • Wang, Z.X.1    Preiss, B.2    Tsou, C.L.3
  • 19
    • 0028609696 scopus 로고
    • Kinetics of irreversible inhibition of creatine kinase during modification by ophthaldehyde
    • Wang, Z.F., Xu, Y.K., and Zhou, H.M. 1994. Kinetics of irreversible inhibition of creatine kinase during modification by ophthaldehyde. Enzyme Protein, 48: 1-9.
    • (1994) Enzyme Protein , vol.48 , pp. 1-9
    • Wang, Z.F.1    Xu, Y.K.2    Zhou, H.M.3
  • 20
    • 0031464741 scopus 로고    scopus 로고
    • Conformational changes of creatine kinase in trifluoroethanol solutions
    • Yang, H.P., and Zhou, H.M. 1997. Conformational changes of creatine kinase in trifluoroethanol solutions. Biochem. Mol. Biol. Int. 43: 1297-1304.
    • (1997) Biochem. Mol. Biol. Int. , vol.43 , pp. 1297-1304
    • Yang, H.P.1    Zhou, H.M.2
  • 21
    • 0020344240 scopus 로고
    • A comparison of denaturation and inactivation rates of creatine kinase in guanidine solutions
    • Yao, Q.Z., Zhou, H.M., Hou, L.X., and Tsou, C.L. 1982. A comparison of denaturation and inactivation rates of creatine kinase in guanidine solutions. Sci. Sin. 25B: 1296-1302.
    • (1982) Sci. Sin. , vol.25 B , pp. 1296-1302
    • Yao, Q.Z.1    Zhou, H.M.2    Hou, L.X.3    Tsou, C.L.4
  • 22
    • 0021755632 scopus 로고
    • Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation
    • Yao, Q.Z., Tian, M., and Tsou, C.L. 1984. Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation. Biochemistry, 23: 2740-2744.
    • (1984) Biochemistry , vol.23 , pp. 2740-2744
    • Yao, Q.Z.1    Tian, M.2    Tsou, C.L.3
  • 23
    • 0030480284 scopus 로고    scopus 로고
    • Inactivation and conformational changes of aminoacyclase in trifluoroethanol solutions
    • Zhang, Y.X., Yan, S.L., and Zhou, H.M. 1996. Inactivation and conformational changes of aminoacyclase in trifluoroethanol solutions. J. Protein Chem. 15: 631-637.
    • (1996) J. Protein Chem. , vol.15 , pp. 631-637
    • Zhang, Y.X.1    Yan, S.L.2    Zhou, H.M.3
  • 24
    • 0034255229 scopus 로고    scopus 로고
    • Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions
    • Zhang, Y.X., Zhu, Y., and Zhou, H.M. 2000. Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions. Int. J. Biochem. Cell Biol. 32: 887-894.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 887-894
    • Zhang, Y.X.1    Zhu, Y.2    Zhou, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.