메뉴 건너뛰기
Biochemistry (Moscow)
Volumn 74, Issue 12, 2009, Pages 1337-1343
PH-dependent urea-induced unfolding of stem bromelain: Unusual stability against urea at neutral pH
Author keywords

Protein stability; Stem bromelain; Urea denaturation
Indexed keywords

BROMELAIN; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; EMISSION SPECTROSCOPY; FREE ENERGY; UREA;
EID: 74849128371     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297909120062     Document Type: Article
Times cited : (9)
References (41)
  • 3
    • 0027749370 scopus 로고
    • 10.1126/science.8235610
    • O. A. Jemmings P. E. Wright 1993 Science 262 892 895 10.1126/science. 8235610
    • (1993) Science , vol.262 , pp. 892-895
    • Jemmings, O.A.1    Wright, P.E.2
  • 4
    • 0024417964 scopus 로고
    • 10.1002/prot.340060202 1:CAS:528:DyaK3cXltVKmuw%3D%3D 2695928
    • K. Kuwajima 1989 Proteins 6 87 103 10.1002/prot.340060202 1:CAS:528:DyaK3cXltVKmuw%3D%3D 2695928
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 5
    • 0023626273 scopus 로고
    • 10.1007/BF00248050 1:CAS:528:DyaL1cXitFyl
    • O. B. Ptitsyn 1987 J. Protein Chem. 6 273 293 10.1007/BF00248050 1:CAS:528:DyaL1cXitFyl
    • (1987) J. Protein Chem. , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 6
    • 0030984867 scopus 로고    scopus 로고
    • 10.1111/j.1432-1033.1997.00328.x
    • J. M. Sanz G. G. Gallego 1997 Eur. J. Biochem. 240 328 335 10.1111/j.1432-1033.1997.00328.x
    • (1997) Eur. J. Biochem. , vol.240 , pp. 328-335
    • Sanz, J.M.1    Gallego, G.G.2
  • 7
    • 0022828086 scopus 로고
    • 10.1016/0378-1119(86)90080-6 1:CAS:528:DyaL2sXhvFSju7c%3D 2881845
    • L. W. Cohen V. M. Coghlan L. C. Dihe 1986 Gene 48 219 227 10.1016/0378-1119(86)90080-6 1:CAS:528:DyaL2sXhvFSju7c%3D 2881845
    • (1986) Gene , vol.48 , pp. 219-227
    • Cohen, L.W.1    Coghlan, V.M.2    Dihe, L.C.3
  • 8
    • 0017846050 scopus 로고
    • 1:CAS:528:DyaE1MXjsFGkuw%3D%3D 687380
    • A. Carne C. H. Moore 1978 Biochem. J. 173 73 83 1:CAS:528: DyaE1MXjsFGkuw%3D%3D 687380
    • (1978) Biochem. J. , vol.173 , pp. 73-83
    • Carne, A.1    Moore, C.H.2
  • 12
    • 0024551586 scopus 로고
    • Stem bromelain: Amino acid sequence and implications for weak binding of cystatin
    • DOI 10.1016/0014-5793(89)81383-3
    • A. Ritonja A. D. Rowan D. J. Buttle N. D. Railings V. Turk A. J. Barett 1989 FEBS Lett. 247 419 424 10.1016/0014-5793(89)81383-3 1:CAS:528: DyaL1MXltFWmtr4%3D 2714443 (Pubitemid 19129290)
    • (1989) FEBS Letters , vol.247 , Issue.2 , 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
  • 13
  • 14
    • 0021770943 scopus 로고
    • 10.1016/0022-2836(84)90467-4 1:CAS:528:DyaL2MXitVensg%3D%3D 6502713
    • I. G. Kamphuis K. H. Kalk M. B. A. Swarte J. Drenth 1984 J. Mol. Biol. 179 233 257 10.1016/0022-2836(84)90467-4 1:CAS:528:DyaL2MXitVensg%3D%3D 6502713
    • (1984) J. Mol. Biol. , vol.179 , pp. 233-257
    • Kamphuis, I.G.1    Kalk, K.H.2    Swarte, M.B.A.3    Drenth, J.4
  • 15
    • 0019156319 scopus 로고
    • Structure of actinidin, after refinement at 1.7 θ resolution
    • DOI 10.1016/0022-2836(80)90255-7
    • E. N. Baker 1980 J. Mol. Biol. 141 441 484 10.1016/0022-2836(80)90255-7 1:CAS:528:DyaL3cXmtleisLo%3D 7003158 (Pubitemid 11227284)
    • (1980) Journal of Molecular Biology , vol.141 , Issue.4 , pp. 441-484
    • Baker, E.N.1
  • 19
    • 0142031484 scopus 로고    scopus 로고
    • Differences in the Unfolding of Procerain Induced by pH, Guanidine Hydrochloride, Urea, and Temperature
    • DOI 10.1021/bi035047m
    • V. K. Dubey M. V. Jagannadham 2003 Biochemistry 42 12287 12297 10.1021/bi035047m 1:CAS:528:DC%2BD3sXns1WmtL8%3D 14567690 (Pubitemid 37296505)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12287-12297
    • Dubey, V.K.1    Jagannadham, M.V.2
  • 21
    • 0037376207 scopus 로고    scopus 로고
    • Procerain, a stable cysteine protease from the latex of Calotropis procera
    • DOI 10.1016/S0031-9422(02)00676-3
    • V. K. Dubey M. V. Jagannadham 2003 Phytochemistry 62 1057 1071 10.1016/S0031-9422(02)00676-3 12591258 (Pubitemid 36323476)
    • (2003) Phytochemistry , vol.62 , Issue.7 , pp. 1057-1071
    • Kumar Dubey, V.1    Jagannadham, M.V.2
  • 23
    • 1042299981 scopus 로고    scopus 로고
    • Structural Basis of the Unusual Stability and Substrate Specificity of Ervatamin C, a Plant Cysteine Protease from Ervatamia coronaria
    • DOI 10.1021/bi0357659
    • P. G. Thakurta S. Biswas C. Chakrabarti M. Sundd M. V. Jagannadham J. K. Dattagupta 2004 Biochemistry 43 1532 1540 10.1021/bi0357659 1:CAS:528: DC%2BD2cXkvVWksw%3D%3D 14769029 (Pubitemid 38200558)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1532-1540
    • Thakurta, P.G.1    Biswas, S.2    Chakrabarti, C.3    Sundd, M.4    Jagannadham, M.V.5    Dattagupta, J.K.6
  • 24
    • 0141706505 scopus 로고    scopus 로고
    • 10.1021/jf026184d 1:CAS:528:DC%2BD3sXnt1Knu7s%3D 14518963
    • B. K. Patel M. V. Jagannadham 2003 J. Agric. Food Chem. 51 6326 6334 10.1021/jf026184d 1:CAS:528:DC%2BD3sXnt1Knu7s%3D 14518963
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 6326-6334
    • Patel, B.K.1    Jagannadham, M.V.2
  • 25
    • 0033843336 scopus 로고    scopus 로고
    • Alcohol-induced conformational transitions in ervatamin C. An α-helix to β-Sheet switchover
    • DOI 10.1023/A:1007010818108
    • M. Sundd S. Kundu M. V. Jagannadham 2000 J. Protein Chem. 3 169 176 10.1023/A:1007010818108 (Pubitemid 30667039)
    • (2000) Journal of Protein Chemistry , vol.19 , Issue.3 , pp. 169-176
    • Sundd, M.1    Kundu, S.2    Jagannadham, M.V.3
  • 27
    • 0014965889 scopus 로고
    • 10.1021/bi00811a012 1:CAS:528:DyaE3cXkt1Wltbs%3D 5442162
    • T. Murachi M. Yamazaki 1970 Biochemistry 9 1935 1938 10.1021/bi00811a012 1:CAS:528:DyaE3cXkt1Wltbs%3D 5442162
    • (1970) Biochemistry , vol.9 , pp. 1935-1938
    • Murachi, T.1    Yamazaki, M.2
  • 28
    • 0036153595 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of stem bromelain at low pH
    • DOI 10.1046/j.0014-2956.2002.02620.x
    • S. K. Haq S. Rasheedi R. H. Khan 2002 Eur. J. Biochem. 269 47 52 10.1046/j.0014-2956.2002.02620.x 1:CAS:528:DC%2BD38XosFCquw%3D%3D 11784297 (Pubitemid 34107338)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.1 , pp. 47-52
    • Haq, S.K.1    Rasheedi, S.2    Khan, R.H.3
  • 29
    • 33845312248 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD28XhtFyrsbzL
    • B. Ahmad R. H. Khan 2006 J. Biochem. (Tokyo) 140 501 508 1:CAS:528:DC%2BD28XhtFyrsbzL
    • (2006) J. Biochem. (Tokyo) , vol.140 , pp. 501-508
    • Ahmad, B.1    Khan, R.H.2
  • 31
    • 0242418209 scopus 로고    scopus 로고
    • Trifluoroethanol-induced molten globule state in stem bromelain
    • DOI 10.1016/S0003-9861(03)00126-7
    • P. Gupta R. H. Khan M. Saleemuddin 2003 Arch. Biochem. Biophys. 413 199 206 10.1016/S0003-9861(03)00126-7 1:CAS:528:DC%2BD3sXjt1KjtL8%3D 12729617 (Pubitemid 36506808)
    • (2003) Archives of Biochemistry and Biophysics , vol.413 , Issue.2 , pp. 199-206
    • Gupta, P.1    Khan, R.H.2    Saleemuddin, M.3
  • 32
    • 33645692570 scopus 로고    scopus 로고
    • 10.1002/bip.20424 1:CAS:528:DC%2BD28XjtVant7k%3D 16345002
    • B. Ahmad M. A. Ansari P. Sen R. H. Khan 2006 Biopolymers 81 350 359 10.1002/bip.20424 1:CAS:528:DC%2BD28XjtVant7k%3D 16345002
    • (2006) Biopolymers , vol.81 , pp. 350-359
    • Ahmad, B.1    Ansari, M.A.2    Sen, P.3    Khan, R.H.4
  • 33
    • 0001798950 scopus 로고    scopus 로고
    • G. Vanhoof W. Cooreman A. Lauwers S. Scharpe (eds). Marcel Dekker Inc. New York
    • Vanhoof, G., Cooreman, W., Lauwers, A., and Scharpe, S. (eds.) (1997) Bromelain in Pharmaceutical Enzymes, Marcel Dekker Inc., New York, pp. 131-147.
    • (1997) Bromelain in Pharmaceutical Enzymes , pp. 131-147
  • 35
    • 0015522150 scopus 로고
    • 10.1021/bi00772a015 1:CAS:528:DyaE3sXht12ltw%3D%3D 4343790
    • Y. H. Chen J. T. Yang H. Martinez 1972 Biochemistry 11 4120 4131 10.1021/bi00772a015 1:CAS:528:DyaE3sXht12ltw%3D%3D 4343790
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.3
  • 36
    • 0025420076 scopus 로고
    • 10.1016/0167-7799(90)90146-O 1:CAS:528:DyaK3cXltFWks7k%3D 1367432
    • C. N. Pace 1990 Trends Biotechnol. 8 93 98 10.1016/0167-7799(90)90146-O 1:CAS:528:DyaK3cXltFWks7k%3D 1367432
    • (1990) Trends Biotechnol. , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 37
    • 0028027707 scopus 로고
    • A kinetic method to evaluate the two-state character of solvent-induced protein denaturation
    • DOI 10.1021/bi00209a025
    • M. Mucke F. X. Schmid 1994 Biochemistry 33 12930 12935 10.1021/bi00209a025 1:STN:280:DyaK2M%2FjsVOiuw%3D%3D 7947699 (Pubitemid 24352884)
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12930-12935
    • Mucke, M.1    Schmid, F.X.2
  • 38
    • 0031808804 scopus 로고    scopus 로고
    • 10.1016/S0006-3495(98)77537-X 1:CAS:528:DyaK1cXktlWmtLk%3D 9649410
    • J. S. Soulages 1998 Biophys. J. 75 484 492 10.1016/S0006-3495(98)77537-X 1:CAS:528:DyaK1cXktlWmtLk%3D 9649410
    • (1998) Biophys. J. , vol.75 , pp. 484-492
    • Soulages, J.S.1
  • 40
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates versus molten globule models for protein folding: Characterization of partially folded intermediates of apomyoglobin
    • DOI 10.1016/S1359-0278(98)00005-4
    • A. L. Fink K. A. Oberg S. Seshadri 1998 Fold. Des. 3 19 25 10.1016/S1359-0278(98)00005-4 1:CAS:528:DyaK1cXhtFSks7k%3D 9502317 (Pubitemid 28085705)
    • (1998) Folding and Design , vol.3 , Issue.1 , pp. 19-25
    • Fink, A.L.1    Oberg, K.A.2    Seshadri, S.3

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.