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Volumn 341, Issue 2, 2006, Pages 620-626

Structural characterization of the papaya cysteine proteinases at low pH

Author keywords

Anthelmintics; Caricain; Chymopapain; Gastrointestinal nematodes; Glycine endopeptidase; Molten globule; Papain; Proteolytic susceptibility

Indexed keywords

CARICAIN EXTRACT; CHYMOPAPAIN; CYSTEINE PROTEINASE; GLYCINE; PAPAIN; PEPSIN A; PLANT EXTRACT; UNCLASSIFIED DRUG;

EID: 31444449434     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.12.210     Document Type: Article
Times cited : (47)

References (29)
  • 1
    • 0031281368 scopus 로고    scopus 로고
    • The global burden of intestinal nematode infections-fifty years on
    • M.S. Chan The global burden of intestinal nematode infections-fifty years on Parasitol. Today 13 1997 438 443
    • (1997) Parasitol. Today , vol.13 , pp. 438-443
    • Chan, M.S.1
  • 3
    • 0034110649 scopus 로고    scopus 로고
    • Drug resistance in human helminths: Current situation and lessons from livestock
    • S. Geerts, and B. Gryseels Drug resistance in human helminths: current situation and lessons from livestock Clin. Microbiol. Rev. 13 2000 207 222
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 207-222
    • Geerts, S.1    Gryseels, B.2
  • 4
    • 13844305828 scopus 로고    scopus 로고
    • Assessment of the anthelmintic effect of natural plant cysteine proteinases against the gastrointestinal nematode Heligmosomoides polygyrus, in vitro
    • G. Stepek, D.J. Buttle, I.R. Duce, A. Lowe, and J.M. Behnke Assessment of the anthelmintic effect of natural plant cysteine proteinases against the gastrointestinal nematode Heligmosomoides polygyrus, in vitro Parasitology 130 2005 203 211
    • (2005) Parasitology , vol.130 , pp. 203-211
    • Stepek, G.1    Buttle, D.J.2    Duce, I.R.3    Lowe, A.4    Behnke, J.M.5
  • 5
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • O.B. Ptitsyn Molten globule and protein folding Adv. Protein Chem. 47 1995 83 122
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-122
    • Ptitsyn, O.B.1
  • 6
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • A.L. Fink, L.J. Calciano, Y. Goto, T. Kurotsu, and D.R. Palleros Classification of acid denaturation of proteins: intermediates and unfolded states Biochemistry 33 1994 12504 12511
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 7
    • 0032573356 scopus 로고    scopus 로고
    • Sequential unfolding of papain in molten globule state
    • F. Edwin, and M.V. Jagannadham Sequential unfolding of papain in molten globule state Biochem. Biophys. Res. Commun. 252 1998 654 660
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 654-660
    • Edwin, F.1    Jagannadham, M.V.2
  • 8
    • 0036153595 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of stem bromelain at low pH
    • S.K. Haq, S. Rasheedi, and R.H. Khan Characterization of a partially folded intermediate of stem bromelain at low pH Eur. Biochem. 269 2002 47 52
    • (2002) Eur. Biochem. , vol.269 , pp. 47-52
    • Haq, S.K.1    Rasheedi, S.2    Khan, R.H.3
  • 9
    • 0036004446 scopus 로고    scopus 로고
    • Acid and chemical induced conformational changes of ervatamin B. Presence of partially structured multiple interactions
    • M. Sundd, S. Kundu, and M.V. Jagannadham Acid and chemical induced conformational changes of ervatamin B. Presence of partially structured multiple interactions J. Biochem. Mol. Biol. 35 2002 143 154
    • (2002) J. Biochem. Mol. Biol. , vol.35 , pp. 143-154
    • Sundd, M.1    Kundu, S.2    Jagannadham, M.V.3
  • 10
    • 0142031484 scopus 로고    scopus 로고
    • Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea, and temperature
    • V.K. Dubey, and M.V. Jagannadham Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea, and temperature Biochemistry 42 2003 12287 12297
    • (2003) Biochemistry , vol.42 , pp. 12287-12297
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 12
    • 0024291085 scopus 로고
    • Detection and characterization by circular dichroism of a stable intermediate state formed in the thermal unfolding of papain
    • A. Hernandez-Arana, and M. Soriano-Garcia Detection and characterization by circular dichroism of a stable intermediate state formed in the thermal unfolding of papain Biochim. Biophys. Acta 954 1988 170 175
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 170-175
    • Hernandez-Arana, A.1    Soriano-Garcia, M.2
  • 13
    • 0017819511 scopus 로고
    • Papain denaturation is not a two-state process
    • E.I. Tiktopulo, and P.L. Privalov Papain denaturation is not a two-state process FEBS Lett. 91 1978 57 58
    • (1978) FEBS Lett. , vol.91 , pp. 57-58
    • Tiktopulo, E.I.1    Privalov, P.L.2
  • 15
    • 0037252893 scopus 로고    scopus 로고
    • N-terminal domain unfolds first in the sequential unfolding of papain
    • Y.V. Sharma, and M.V. Jagannadham N-terminal domain unfolds first in the sequential unfolding of papain Protein Pept. Lett. 10 2003 83 90
    • (2003) Protein Pept. Lett. , vol.10 , pp. 83-90
    • Sharma, Y.V.1    Jagannadham, M.V.2
  • 16
    • 0033517819 scopus 로고    scopus 로고
    • Structural characterization of a highly stable cysteine protease ervatamin C
    • S. Kundu, M. Sundd, and M.V. Jagannadham Structural characterization of a highly stable cysteine protease ervatamin C Biochem. Biophys. Res. Commun. 264 1999 635 642
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 635-642
    • Kundu, S.1    Sundd, M.2    Jagannadham, M.V.3
  • 18
    • 2342668327 scopus 로고    scopus 로고
    • Estimating the degree of expansion in the transition state for protein unfolding: Analysis of the pH dependence of the rate constant for caricain denaturation
    • L. Lopez-Arenas, S. Solis-Mendiola, and A. Hernandez-Arana Estimating the degree of expansion in the transition state for protein unfolding: analysis of the pH dependence of the rate constant for caricain denaturation Biochemistry 38 1999 15936 15943
    • (1999) Biochemistry , vol.38 , pp. 15936-15943
    • Lopez-Arenas, L.1    Solis-Mendiola, S.2    Hernandez-Arana, A.3
  • 20
    • 1542332689 scopus 로고    scopus 로고
    • Proteolytic activity and immunogenicity of oral bromelain within the gastrointestinal tract of mice
    • L.P. Hale Proteolytic activity and immunogenicity of oral bromelain within the gastrointestinal tract of mice Int. Immunopharmacol. 4 2004 255 264
    • (2004) Int. Immunopharmacol. , vol.4 , pp. 255-264
    • Hale, L.P.1
  • 21
  • 22
    • 0000478993 scopus 로고
    • Fragmentation of bovine serum albumin by pepsin
    • G. Weber, and L.B. Young Fragmentation of bovine serum albumin by pepsin J. Biol. Chem. 239 1964 1415 1423
    • (1964) J. Biol. Chem. , vol.239 , pp. 1415-1423
    • Weber, G.1    Young, L.B.2
  • 23
    • 0030022922 scopus 로고
    • S-Pegylthio-papain, a versatile intermediate for the preparation of the fully active form of the cysteine proteinase archetype
    • M. Azarkan, R.T. Wintjens, N. Smolders, M. Nijs, and Y. Looze S-Pegylthio-papain, a versatile intermediate for the preparation of the fully active form of the cysteine proteinase archetype J. Chromatogr. A 724 1995 185 192
    • (1995) J. Chromatogr. a , vol.724 , pp. 185-192
    • Azarkan, M.1    Wintjens, R.T.2    Smolders, N.3    Nijs, M.4    Looze, Y.5
  • 25
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set Anal. Biochem. 287 2000 252 260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 26
    • 0024066667 scopus 로고
    • The thiol proteinases from the latex of Carica papaya L. II. the primary structure of papaya proteinase omega
    • T. Dubois, T. Kleinschmidt, A.G. Schnek, Y. Looze, and G. Braunitzer The thiol proteinases from the latex of Carica papaya L. II. The primary structure of papaya proteinase omega Biol. Chem. Hoppe-Seyler 369 1988 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
  • 27
    • 31444450716 scopus 로고    scopus 로고
    • Histidine-aromatic interactions in proteins and protein-ligand complexes: Quantum chemical study of X-ray and model structures
    • E. Cauët, M. Rooman, R. Wintjens, J. Liévin, and C. Biot Histidine-aromatic interactions in proteins and protein-ligand complexes: quantum chemical study of X-ray and model structures J. Chem. Theory Comput. 1 2005 472 483
    • (2005) J. Chem. Theory Comput. , vol.1 , pp. 472-483
    • Cauët, E.1    Rooman, M.2    Wintjens, R.3    Liévin, J.4    Biot, C.5
  • 28
    • 31444448332 scopus 로고
    • Fluorometric detection of histidine-tryptophan complexes in peptides and proteins
    • M. Shinitzky, and R. Goldman Fluorometric detection of histidine-tryptophan complexes in peptides and proteins J. Biol. Chem. 239 1964 1415 1423
    • (1964) J. Biol. Chem. , vol.239 , pp. 1415-1423
    • Shinitzky, M.1    Goldman, R.2
  • 29
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • V.N. Uversky What does it mean to be natively unfolded? FEBS Lett. 269 2002 2 12
    • (2002) FEBS Lett. , vol.269 , pp. 2-12
    • Uversky, V.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.