메뉴 건너뛰기




Volumn 33, Issue 5-6 SPECL.ISSUE, 2007, Pages 463-475

Thermal characterization and cytotoxicity of complexes formed by papain and cyclodextrin

Author keywords

Cyclodextrin; Cytotoxicity; Differential scanning calorimetry; Fibroblasts; Human keratinocytes; Papain

Indexed keywords


EID: 77953522942     PISSN: 00920606     EISSN: 15730689     Source Type: Journal    
DOI: 10.1007/s10867-008-9098-8     Document Type: Article
Times cited : (4)

References (24)
  • 2
    • 0021770943 scopus 로고
    • Structure of papain refined at 1.65 angstrom resolution
    • doi:10.1016/0022-2836(84)90467-4
    • Kamphuis, I.G., Kalk, K.H., Swarte, M.B.A., Drent, H.J.: Structure of papain refined at 1.65 angstrom resolution. J. Mol. Biol. 179, 233-256 (1984). doi:10.1016/0022-2836(84)90467-4
    • (1984) J. Mol. Biol. , vol.179 , pp. 233-256
    • Kamphuis, I.G.1    Kalk, K.H.2    Swarte, M.B.A.3    Drent, H.J.4
  • 3
    • 0038653828 scopus 로고    scopus 로고
    • 13th edn. Merck Research Laboratories, Whitehouse Station, NJ
    • O'Neil, M.J.: The Merck Index, 13th edn. Merck Research Laboratories, Whitehouse Station, NJ (2001)
    • (2001) The Merck Index
    • O'Neil, M.J.1
  • 4
    • 34548290876 scopus 로고    scopus 로고
    • Mechanism of solvent induced thermal stabilization of papain
    • doi:10.1016/j.ijbiomac.2007.05.009
    • Sathish, H.A., Kumar, P.R., Prakash, V.: Mechanism of solvent induced thermal stabilization of papain. Int. J. Biol. Macromol. 41, 383-390 (2007). doi:10.1016/j.ijbiomac.2007.05.009
    • (2007) Int. J. Biol. Macromol. , vol.41 , pp. 383-390
    • Sathish, H.A.1    Kumar, P.R.2    Prakash, V.3
  • 5
    • 0026093558 scopus 로고
    • Denaturation studies of active-site labeled papain using electron paramagnetic resonance and fluorescence spectroscopy
    • Zhuang, P., Butterfield, D.A.: Denaturation studies of active-site labeled papain using electron paramagnetic resonance and fluorescence spectroscopy. Biophys. J. 60, 623-628 (1991)
    • (1991) Biophys. J. , vol.60 , pp. 623-628
    • Zhuang, P.1    Butterfield, D.A.2
  • 6
    • 0030182390 scopus 로고    scopus 로고
    • Unfolding mechanism and stability of immobilized papain
    • doi:10.1007/BF01982682
    • Rialdi, G., Battistel, E.: Unfolding mechanism and stability of immobilized papain. J. Therm. Anal. 47, 17-25 (1996). doi:10.1007/BF01982682
    • (1996) J. Therm. Anal. , vol.47 , pp. 17-25
    • Rialdi, G.1    Battistel, E.2
  • 7
    • 0028880786 scopus 로고
    • Effects of β-cyclodextrins on the skin: Implications for the transdermal delivery of piribedil and a novel cognition enhancing-drug, S-9977
    • doi:10.1016/0928-0987(95)00020-0
    • Legendre, J.Y., Rault, I., Petit, A., Luijten, W., Demuynck, I., Horvath, S., Ginot, Y.M., Cuine, A.: Effects of β-cyclodextrins on the skin: implications for the transdermal delivery of piribedil and a novel cognition enhancing-drug, S-9977. Eur. J. Pharm. Sci. 3, 311-322 (1995). doi:10.1016/0928-0987(95)00020-0
    • (1995) Eur. J. Pharm. Sci. , vol.3 , pp. 311-322
    • Legendre, J.Y.1    Rault, I.2    Petit, A.3    Luijten, W.4    Demuynck, I.5    Horvath, S.6    Ginot, Y.M.7    Cuine, A.8
  • 8
    • 0036890313 scopus 로고    scopus 로고
    • Biotechnological applications of cyclodextrins
    • doi:10.1016/S0734-9750(02)00020-4
    • Singh, M., Sharma, R., Banerjee, U.C.: Biotechnological applications of cyclodextrins. Biotechnol. Adv. 20, 341-359 (2002). doi:10.1016/S0734-9750(02) 00020-4
    • (2002) Biotechnol. Adv. , vol.20 , pp. 341-359
    • Singh, M.1    Sharma, R.2    Banerjee, U.C.3
  • 9
    • 0027336218 scopus 로고
    • Factors effecting the thermostability of cysteine proteinases from Carica papaya
    • doi:10.1111/j.1432-1033.1993.tb17904.x
    • Sumner, I.G., Harris, G.W., Taylor, M.A.J., Pickersgill, R.W., Owen, A.J., Goodenough, W.: Factors effecting the thermostability of cysteine proteinases from Carica papaya. Eur. J. Biochem. 214, 129-134 (1993). doi:10.1111/j.1432-1033.1993.tb17904.x
    • (1993) Eur. J. Biochem. , vol.214 , pp. 129-134
    • Sumner, I.G.1    Harris, G.W.2    Taylor, M.A.J.3    Pickersgill, R.W.4    Owen, A.J.5    Goodenough, W.6
  • 10
    • 33846596723 scopus 로고    scopus 로고
    • Thermodynamics of proteins in unusual environments
    • doi:10.1016/j.bpc.2006.05.029
    • Rialdi, G., Battistel, E.: Thermodynamics of proteins in unusual environments. Biophys. Chem. 126, 65-79 (2006). doi:10.1016/j.bpc.2006.05.029
    • (2006) Biophys. Chem. , vol.126 , pp. 65-79
    • Rialdi, G.1    Battistel, E.2
  • 12
    • 0000875424 scopus 로고    scopus 로고
    • Applications of scanning microcalorimetry in biophysics and biochemistry
    • doi:10.1016/S0040-6031(97)00238-4
    • Shnyrov, V.L., Sanchez-Ruiz, J.M., Boiko, B.N., Zhadan, G.G., Permyakov, E.A.: Applications of scanning microcalorimetry in biophysics and biochemistry. Thermochim. Acta 302, 165-180 (1997). doi:10.1016/S0040-6031(97)00238-4
    • (1997) Thermochim. Acta , vol.302 , pp. 165-180
    • Shnyrov, V.L.1    Sanchez-Ruiz, J.M.2    Boiko, B.N.3    Zhadan, G.G.4    Permyakov, E.A.5
  • 15
    • 0024291085 scopus 로고
    • Detection and characterization by circular dichroism of a stable intermediate state formed in the thermal unfolding of papain
    • Hernández-Arana, A., Soriano-Garcia, M.: 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)
    • (1988) Biochim. Biophys. Acta , vol.954 , pp. 170-175
    • Hernández-Arana, A.1    Soriano-Garcia, M.2
  • 16
    • 13844321001 scopus 로고    scopus 로고
    • Stabilization of α-chymotrypsin by chemical modification with monoamine cyclodextrin
    • doi:10.1016/j.procbio.2004.07.023
    • Fernández, M., Fragoso, A., Cao, R., Villalonga, R.: Stabilization of α-chymotrypsin by chemical modification with monoamine cyclodextrin. Process Biochem. 40, 2091-2094 (2005). doi:10.1016/j.procbio.2004.07.023
    • (2005) Process Biochem. , vol.40 , pp. 2091-2094
    • Fernández, M.1    Fragoso, A.2    Cao, R.3    Villalonga, R.4
  • 17
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee, J.C., Timasheff, S.N.: The stabilization of proteins by sucrose. J. Biol. Chem. 256, 7193-7201 (1981)
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 18
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • doi:10.1021/bi00268a033
    • Arakawa, T., Timasheff, S.N.: Stabilization of protein structure by sugars. Biochemistry 21, 6536-6544 (1982). doi:10.1021/bi00268a033
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 19
    • 1942470488 scopus 로고    scopus 로고
    • Cyclodextrins and their uses: A review
    • doi:10.1016/S0032-9592(03)00258-9
    • Martin Del Valle, E.M.: Cyclodextrins and their uses: a review. Process Biochem. 39, 1033-1046 (2004). doi:10.1016/S0032-9592(03)00258-9
    • (2004) Process Biochem. , vol.39 , pp. 1033-1046
    • Martin Del Valle, E.M.1
  • 20
    • 0034604764 scopus 로고    scopus 로고
    • Cyclodextrins: A versatile tool in separation science
    • doi:10.1016/S0378-4347(00)00057-8
    • Schneiderman, E., Stalcup, A.M.: Cyclodextrins: a versatile tool in separation science. J. Chromatogr. B 745, 83-102 (2000). doi:10.1016/S0378- 4347(00)00057-8
    • (2000) J. Chromatogr. B , vol.745 , pp. 83-102
    • Schneiderman, E.1    Stalcup, A.M.2
  • 21
    • 0346461917 scopus 로고    scopus 로고
    • Introduction and general overview of cyclodextrin chemistry
    • doi:10.1021/cr970022c
    • Szetjli, J.: Introduction and general overview of cyclodextrin chemistry. Chem. Rev. 98, 1743-1753 (1998). doi:10.1021/cr970022c
    • (1998) Chem. Rev. , vol.98 , pp. 1743-1753
    • Szetjli, J.1
  • 22
    • 84863817030 scopus 로고    scopus 로고
    • Promega: Technical Bulletin Updated 12/2006 Cited 5 Dec 2005
    • ® aqueous non-radiactive cell proliferation assay. Updated 12/2006. http://www.promega.com/enotes/applicattions/sap0017-print.htm. Cited 5 Dec 2005 (2005)
    • (2005) ® Aqueous Non-radiactive Cell Proliferation Assay


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.