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Volumn 141, Issue 2, 2007, Pages 251-259

Identification and characterization of functional intermediates of stem bromelain during urea and guanidine hydrochloride unfolding

Author keywords

Circular dichroism; Cysteine protease; Functional intermediate state; Intrinsic fluorescence; Proteolytic activity

Indexed keywords

ACRYLAMIDE; BROMELAIN; GUANIDINE; TRYPTOPHAN; UREA;

EID: 34249068231     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm026     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates versus molten globule model for protein folding: Characterization of partially folded intermediates of apomyoglobin
    • Fink, A.L., Oberg, K.A., and Seshadri, S. (1997) Discrete intermediates versus molten globule model for protein folding: characterization of partially folded intermediates of apomyoglobin. Fold. Des. 3, 19-25
    • (1997) Fold. Des , vol.3 , pp. 19-25
    • Fink, A.L.1    Oberg, K.A.2    Seshadri, S.3
  • 2
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalove, P.L. (1996) Intermediate states in protein folding. Mol. Biol. 258, 707-725
    • (1996) Mol. Biol , vol.258 , pp. 707-725
    • Privalove, P.L.1
  • 3
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin, R.L. (1996) On-pathway versus off-pathway folding intermediates. Fold. Des. 1, 1-8
    • (1996) Fold. Des , vol.1 , pp. 1-8
    • Baldwin, R.L.1
  • 4
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai, M. and Kuwajima, K. (2000) Role of the molten globule state in protein folding. Adv. Protein. Chem. 53, 209-271
    • (2000) Adv. Protein. Chem , vol.53 , pp. 209-271
    • Arai, M.1    Kuwajima, K.2
  • 5
    • 0027399210 scopus 로고
    • The protein import machinery of mitochondria
    • Schartz, G. (1993) The protein import machinery of mitochondria. Protein Sci. 2, 141-146
    • (1993) Protein Sci , vol.2 , pp. 141-146
    • Schartz, G.1
  • 6
    • 0022828086 scopus 로고
    • Cloning and sequencing of papain-encoding cDNA
    • Cohen, L.W., Coghlan, V.M., and Dihel, L.C. (1986) Cloning and sequencing of papain-encoding cDNA. Gene 48, 21-227
    • (1986) Gene , vol.48 , pp. 21-227
    • Cohen, L.W.1    Coghlan, V.M.2    Dihel, L.C.3
  • 7
    • 0017846050 scopus 로고
    • The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis
    • Carne, A. and Moore, C.H. (1978) The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis. Biochem. J. 173, 73-83
    • (1978) Biochem. J , vol.173 , pp. 73-83
    • Carne, A.1    Moore, C.H.2
  • 8
    • 0024066667 scopus 로고
    • The thiol proteinases from the latex of Carica papaya L. III. The primary structure of proteinase omega
    • Dubois, T., Kleinschmidt, T., Schnek, A.G., Looze, Y., and Braunitzer, G. (1988) The thiol proteinases from the latex of Carica papaya L. III. The primary structure of proteinase omega. Biol. Chem. Hoppe-Seyler 369, 741-754
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 741-754
    • Dubois, T.1    Kleinschmidt, T.2    Schnek, A.G.3    Looze, Y.4    Braunitzer, G.5
  • 9
    • 0025008745 scopus 로고
    • The amino acid sequence of chymopapain from Carica papaya
    • Watson, D.C., Yaguchi, M., and Lynn, K.R. (1990) The amino acid sequence of chymopapain from Carica papaya. Biochem. J. 266, 75-81
    • (1990) Biochem. J , vol.266 , pp. 75-81
    • Watson, D.C.1    Yaguchi, M.2    Lynn, K.R.3
  • 10
    • 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 Barett, A.J. (1989) Stem bromelain: amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247, 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    Barett, A.J.6
  • 12
    • 0019156319 scopus 로고
    • Structure of actinidin after refinement at 1.7 AÊ resolution
    • Baker, E.N. (1980) Structure of actinidin after refinement at 1.7 AÊ resolution. J. Mol. Biol. 141, 441-484
    • (1980) J. Mol. Biol , vol.141 , pp. 441-484
    • Baker, E.N.1
  • 13
  • 14
    • 0027453694 scopus 로고
    • Cooperativity in the unfolding transitions of cysteine proteinases. Calorimetric study of the heat denaturation of chymopapain and papain
    • Mendiola, S.S., Dom_ýnguez, A.R., and Arana, A.H. (1993) Cooperativity in the unfolding transitions of cysteine proteinases. Calorimetric study of the heat denaturation of chymopapain and papain. Biochim. Biophys. Acta. 1203, 121-125
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 121-125
    • Mendiola, S.S.1    Dom-ýnguez, A.R.2    Arana, A.H.3
  • 15
    • 0024291085 scopus 로고
    • Detection and characterization by circular dichroism of a stable intermediate state formed in the thermal unfolding of papain
    • Hernandez-Arana, A. and Soriano-Garcia, M. (1988) Detection and characterization by circular dichroism of a stable intermediate state formed in the thermal unfolding of papain. Biochim. Biophys. Acta. 954, 170-175
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 170-175
    • Hernandez-Arana, A.1    Soriano-Garcia, M.2
  • 16
    • 0028952019 scopus 로고
    • The thermal denaturaton of stem bromelain is consistent with an irreversible two-state model
    • Arroyo-Reyna, A. and Hernandez-Arana, A. (1995) The thermal denaturaton of stem bromelain is consistent with an irreversible two-state model. Biochem. Biophys. Acta. 1248, 123-128
    • (1995) Biochem. Biophys. Acta , vol.1248 , pp. 123-128
    • Arroyo-Reyna, A.1    Hernandez-Arana, A.2
  • 17
    • 0014965889 scopus 로고
    • Changes in conformation and enzymatic activity of stem bromelain in alkaline media
    • Murachi, T. and Yamazaki, M. (1970) Changes in conformation and enzymatic activity of stem bromelain in alkaline media. Biochemistry 9, 1935-1938
    • (1970) Biochemistry , vol.9 , pp. 1935-1938
    • Murachi, T.1    Yamazaki, M.2
  • 18
    • 0036153595 scopus 로고    scopus 로고
    • Characterization of partially folded intermediate of stem bromelaine at low pH
    • Haq, S.K., Rasheedi, S., and Khan, R.H. (2002) Characterization of partially folded intermediate of stem bromelaine at low pH. Eur. J. Biochem. 269, 47-52
    • (2002) Eur. J. Biochem , vol.269 , pp. 47-52
    • Haq, S.K.1    Rasheedi, S.2    Khan, R.H.3
  • 19
    • 4944221022 scopus 로고    scopus 로고
    • Influence of salts and alcohols on the conformation of partially folded state of stem bromelain at low pH
    • Haq, S.K., Rasheedi, S., Sharma, P., Ahmad, B., and Khan, R.H. (2005) Influence of salts and alcohols on the conformation of partially folded state of stem bromelain at low pH. Int. J. Biochem. Cell. Biol. 37, 361-374
    • (2005) Int. J. Biochem. Cell. Biol , vol.37 , pp. 361-374
    • Haq, S.K.1    Rasheedi, S.2    Sharma, P.3    Ahmad, B.4    Khan, R.H.5
  • 20
    • 33645692570 scopus 로고    scopus 로고
    • Low versus high molecular weight poly ethylene glycol induced states of stem bromelain at low pH: Stabilization of molten globule and unfolded states
    • Ahmad, B., Ansari, M.A., Sen, P., and Khan, R.H. (2006) Low versus high molecular weight poly ethylene glycol induced states of stem bromelain at low pH: stabilization of molten globule and unfolded states. Biopolymers 81, 350-359
    • (2006) Biopolymers , vol.81 , pp. 350-359
    • Ahmad, B.1    Ansari, M.A.2    Sen, P.3    Khan, R.H.4
  • 21
    • 0001798950 scopus 로고    scopus 로고
    • Lauwers, A. and Scharpe, S. eds Marcel Dekker Inc, New York
    • Vanhoof, G. and Cooreman, W.B. (1997) Pharmaceutical Enzymes (Lauwers, A. and Scharpe, S. eds) Marcel Dekker Inc., New York
    • (1997) Pharmaceutical Enzymes
    • Vanhoof, G.1    Cooreman, W.B.2
  • 22
    • 0028053016 scopus 로고
    • Equilibrium unfolding studies of barstar: Evidence for an alternative conformation which resembles a molten globule
    • Khurana, R. and Udgaonkar, J.B. (1994) Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule. Biochemistry 33, 106-115
    • (1994) Biochemistry , vol.33 , pp. 106-115
    • Khurana, R.1    Udgaonkar, J.B.2
  • 23
    • 34249082227 scopus 로고    scopus 로고
    • Demeester, J., Dekeyser, P.M., Samyn, N., Sierens, W., and lauwers, A. (1997) Bromelain in Pharmaceutical Enzymes (Lauwers, A. and Scharpe, S. eds) pp. 365-368s, Marcel Dekker Inc., New York
    • Demeester, J., Dekeyser, P.M., Samyn, N., Sierens, W., and lauwers, A. (1997) Bromelain in Pharmaceutical Enzymes (Lauwers, A. and Scharpe, S. eds) pp. 365-368s, Marcel Dekker Inc., New York
  • 24
    • 0345550275 scopus 로고    scopus 로고
    • Comparison of protein precipitation method for sample preparation prior to proteomic analysis
    • Jiang, L., He, L., and Fountoulakis, M. (2004) Comparison of protein precipitation method for sample preparation prior to proteomic analysis. J. Chromatogr. A. 1023, 317-320
    • (2004) J. Chromatogr. A , vol.1023 , pp. 317-320
    • Jiang, L.1    He, L.2    Fountoulakis, M.3
  • 25
    • 0015522150 scopus 로고
    • Determination of the secondary structure of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y.H., Yang, J.T., and Martinez, H. (1972) Determination of the secondary structure of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.3
  • 26
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M.R. and Ghiron, C.A. (1982) Fluorescence quenching studies with proteins. Anal. Biochem. 114, 199-227
    • (1982) Anal. Biochem , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 28
    • 0014011601 scopus 로고
    • Pepsin from pepsinogen. Preparation and properties
    • Rajagopalan, T.G., Moore, S., and Stein, W.H. (1966) Pepsin from pepsinogen. Preparation and properties. J. Biol. Chem. 242, 4940-1950
    • (1966) J. Biol. Chem , vol.242 , pp. 4940-1950
    • Rajagopalan, T.G.1    Moore, S.2    Stein, W.H.3
  • 29
    • 0014669425 scopus 로고
    • Cleavage of one specific disulfide bond in papain
    • Sharpira, E. and Arnon, R. (1969) Cleavage of one specific disulfide bond in papain. J. Biol. Chem. 244, 4989-4994
    • (1969) J. Biol. Chem , vol.244 , pp. 4989-4994
    • Sharpira, E.1    Arnon, R.2
  • 30
    • 0014718113 scopus 로고
    • Protein denaturation, Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970) Protein denaturation, Theoretical models for the mechanism of denaturation. Adv. Protein. Chem. 24, 1-95
    • (1970) Adv. Protein. Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 32
    • 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 Arreguin-Espinosa, R. (1994) Circular dichroism of stem bromelain a third spectral class within the family of cysteine proteinases. Biochem. J 300, 107-110
    • (1994) Biochem. J , vol.300 , pp. 107-110
    • Arroyo-Reyna, A.1    Hernandez-Arana, A.2    Arreguin-Espinosa, R.3
  • 33
    • 0025305682 scopus 로고
    • Modulation of spinach chloroplast NADP glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions
    • Wolosiuk, R.A. and Stein, M. (1990) Modulation of spinach chloroplast NADP glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions. Arch. Biochem. Biophy 279, 70-77
    • (1990) Arch. Biochem. Biophy , vol.279 , pp. 70-77
    • Wolosiuk, R.A.1    Stein, M.2
  • 34
    • 0029917031 scopus 로고    scopus 로고
    • Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site
    • Fan, Y.-X., Ju, M., Zhou, J.-M., and Tsou, C.-L. (1996) Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site. Biochem. J. 315, 97-102
    • (1996) Biochem. J , vol.315 , pp. 97-102
    • Fan, Y.-X.1    Ju, M.2    Zhou, J.-M.3    Tsou, C.-L.4
  • 35
    • 0031424798 scopus 로고    scopus 로고
    • The influence of chaotropic reagents on neuronal nitric oxide synthase and its flavoprotein module. Urea and guanidine hydrochloride stimulate NADPH-cytochrome c reductase activity of both proteins
    • Narayanasami, R., Nishimura, J.S., McMillan, K., Roman, L.J., Shea, T.M., Robida, A.M., Horowitz, P.M., and Masters, B.S.S. (1997) The influence of chaotropic reagents on neuronal nitric oxide synthase and its flavoprotein module. Urea and guanidine hydrochloride stimulate NADPH-cytochrome c reductase activity of both proteins. Nitric Oxide 1, 39-49
    • (1997) Nitric Oxide , vol.1 , pp. 39-49
    • Narayanasami, R.1    Nishimura, J.S.2    McMillan, K.3    Roman, L.J.4    Shea, T.M.5    Robida, A.M.6    Horowitz, P.M.7    Masters, B.S.S.8
  • 36
    • 0032523902 scopus 로고    scopus 로고
    • Enhancement of transcriptional activity of T7 RNA polymerase by guanidine hydrochloride
    • Das, M. and Dasgupta, D. (1998) Enhancement of transcriptional activity of T7 RNA polymerase by guanidine hydrochloride. FEBS Lett 427, 337-340
    • (1998) FEBS Lett , vol.427 , pp. 337-340
    • Das, M.1    Dasgupta, D.2
  • 37
    • 0033616154 scopus 로고    scopus 로고
    • Enhancement of lipocalin-type prostaglandin D synthase enzyme activity by guanidine hydrochloride
    • Inui, T., Ohkubo, T., Urade, Y., and Hayaishi, O. (1999) Enhancement of lipocalin-type prostaglandin D synthase enzyme activity by guanidine hydrochloride. Biochem. Biophys. Res. Commun. 266, 641-646
    • (1999) Biochem. Biophys. Res. Commun , vol.266 , pp. 641-646
    • Inui, T.1    Ohkubo, T.2    Urade, Y.3    Hayaishi, O.4
  • 38
    • 0034984373 scopus 로고    scopus 로고
    • Thermostability of proteins from Thermotoga maritima
    • Jaenicke, R. and Böhm, G. (2001) Thermostability of proteins from Thermotoga maritima. Methods Enzymol. 334, 438-469
    • (2001) Methods Enzymol , vol.334 , pp. 438-469
    • Jaenicke, R.1    Böhm, G.2
  • 39
    • 0142031484 scopus 로고    scopus 로고
    • Difference in unfolding of procerain induced by pH, guanidine hydrochloride, urea and temperature
    • Dubey, V.K. and Jagannadham, M.V. (2003) Difference in unfolding of procerain induced by pH, guanidine hydrochloride, urea and temperature. Biochemistry 42, 12287-12297
    • (2003) Biochemistry , vol.42 , pp. 12287-12297
    • Dubey, V.K.1    Jagannadham, M.V.2


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