메뉴 건너뛰기




Volumn 46, Issue 7, 1998, Pages 2546-2553

The pH Dependence of the Structural Stability of Patatin

Author keywords

Patatin; pH dependence; Solanum tuberosum; Structural stability

Indexed keywords

SOLANUM TUBEROSUM; TUBEROSUM;

EID: 0006863740     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf980034e     Document Type: Article
Times cited : (43)

References (40)
  • 1
    • 0025234587 scopus 로고
    • pH-Induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson, D. E,; Becktel, W. J.; Dahlquist, F. W. pH-Induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 1990, 29, 2403-2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 2
    • 0019394794 scopus 로고
    • Interaction of 8-anilino-1-naphthalenesulfonate with rod outer segment membrane
    • Andley, U. P.; Chakrabarti, B. Interaction of 8-anilino-1-naphthalenesulfonate with rod outer segment membrane. Biochemistry 1981, 20, 1687-1693.
    • (1981) Biochemistry , vol.20 , pp. 1687-1693
    • Andley, U.P.1    Chakrabarti, B.2
  • 3
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. J.; Schellman, J. A. Protein stability curves. Biopolymers 1987, 26, 1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 4
    • 0030088058 scopus 로고    scopus 로고
    • Effects of physicochemical factors on the secondary structure of β-lactoglobulin
    • Boye, J. I.; Ismail, A. A.; Alli, I. Effects of physicochemical factors on the secondary structure of β-lactoglobulin. J. Dairy Res. 1996, 63, 97-109.
    • (1996) J. Dairy Res. , vol.63 , pp. 97-109
    • Boye, J.I.1    Ismail, A.A.2    Alli, I.3
  • 5
    • 0002956855 scopus 로고    scopus 로고
    • Thermal denaturation and coagulation of proteins
    • Damodaran, S., Paraf, A.; Eds.; Marcel DekK-ker: New York
    • Boye, J. I.; Ma, C.-Y.; Harwalkar, V. R. Thermal denaturation and coagulation of proteins. In Food proteins and their applications; Damodaran, S., Paraf, A.; Eds.; Marcel DekK-ker: New York, 1997.
    • (1997) Food Proteins and Their Applications
    • Boye, J.I.1    Ma, C.-Y.2    Harwalkar, V.R.3
  • 6
    • 0023658628 scopus 로고
    • pH Dependence of bacteriorhodopsin thermal unfolding
    • Brouillette, C. G.; Muccio, D. D.; Finney, T. K. pH Dependence of bacteriorhodopsin thermal unfolding, Biochemistry 1987, 26, 7431-7438.
    • (1987) Biochemistry , vol.26 , pp. 7431-7438
    • Brouillette, C.G.1    Muccio, D.D.2    Finney, T.K.3
  • 8
    • 0031030973 scopus 로고    scopus 로고
    • pH-Dependent conformational changes in Escherichia Coli dihydrofolate reductase revealed by Raman difference spectroscopy
    • Chen, Y.-Q.; Kraut, J.; Callender, R. pH-Dependent conformational changes in Escherichia Coli dihydrofolate reductase revealed by Raman difference spectroscopy. Biophys. J. 1997, 72, 936-941.
    • (1997) Biophys. J. , vol.72 , pp. 936-941
    • Chen, Y.-Q.1    Kraut, J.2    Callender, R.3
  • 10
    • 0002503849 scopus 로고    scopus 로고
    • Food proteins: An overview
    • Damodaran, S., Paraf, A., Eds.; Marcel Dekker: New York
    • Damodaran, S. Food proteins: An overview. In Food proteins and their applications; Damodaran, S., Paraf, A., Eds.; Marcel Dekker: New York, 1997.
    • (1997) Food Proteins and Their Applications
    • Damodaran, S.1
  • 11
    • 0028921969 scopus 로고
    • Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli
    • Das, B. K.; Bhattacharyya, T.; Roy, S. Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli. Biochemistry 1995, 34, 5242-5247.
    • (1995) Biochemistry , vol.34 , pp. 5242-5247
    • Das, B.K.1    Bhattacharyya, T.2    Roy, S.3
  • 12
    • 0028598299 scopus 로고
    • Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application
    • de Jongh, H. H. J.; Goormaghtigh, E.; Killian, A. Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application. Biochemistry 1994, 33, 14521-14528.
    • (1994) Biochemistry , vol.33 , pp. 14521-14528
    • De Jongh, H.H.J.1    Goormaghtigh, E.2    Killian, A.3
  • 13
    • 0000473598 scopus 로고
    • Wax ester formation catalyzed by isoenzymes of lipolytic acyl hydrolase
    • Dennis, S.; Galliard, T. Wax ester formation catalyzed by isoenzymes of lipolytic acyl hydrolase. Phytochemistry 1974, 13, 2469-2473.
    • (1974) Phytochemistry , vol.13 , pp. 2469-2473
    • Dennis, S.1    Galliard, T.2
  • 14
    • 0017718187 scopus 로고
    • Stability of of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes
    • Ellwel, M. L.; Schellman, J. A. Stability of of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. Biochim. Biophys. Acta 1977, 494, 367-383.
    • (1977) Biochim. Biophys. Acta , vol.494 , pp. 367-383
    • Ellwel, M.L.1    Schellman, J.A.2
  • 15
    • 0343907365 scopus 로고    scopus 로고
    • The effect of heat- and acid-treatment on the structure of rapeseed albumin (napin)
    • Folawiyo, Y. L.; Owusu Apenten, R. K. The effect of heat- and acid-treatment on the structure of rapeseed albumin (napin). Food Chem. 1996, 58, 237-243.
    • (1996) Food Chem. , vol.58 , pp. 237-243
    • Folawiyo, Y.L.1    Owusu Apenten, R.K.2
  • 16
    • 0024963570 scopus 로고
    • Conformational states of a-lactamase: Molten-globule states at acidie and alkaline pH with high salt
    • Goto, Y.; Fink, A. L. Conformational states of a-lactamase: Molten-globule states at acidie and alkaline pH with high salt. Biochemistry 1989, 28, 945-952.
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 17
    • 0028174361 scopus 로고
    • Energetics of a-lactalbumin states: A calorimetric and statistical thermodynamic study
    • Griko, Y. V.; Freire, E.; Privalov, P. L. Energetics of a-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 1994, 33, 1889-1899.
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko, Y.V.1    Freire, E.2    Privalov, P.L.3
  • 18
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey, J. P., Jr.; Johnson, W. C., Jr. Information content in the circular dichroism of proteins. Biochemistry 1981, 20, 1085-1094.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 19
    • 0028944303 scopus 로고
    • Thermoinactivation of cellobiohydrolase I from Trichoderma reesei QM 9414
    • Jiménez, J.; Domínguez, J. M.; Castillón, M. P.; Acebal, C. Thermoinactivation of cellobiohydrolase I from Trichoderma reesei QM 9414. Carbohydr. Res. 1995, 268, 257-266.
    • (1995) Carbohydr. Res. , vol.268 , pp. 257-266
    • Jiménez, J.1    Domínguez, J.M.2    Castillón, M.P.3    Acebal, C.4
  • 20
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson, W. C., Jr. Secondary structure of proteins through circular dichroism spectroscopy. Annu. Rev. Biophys. Chem. 1988, 17, 145-166.
    • (1988) Annu. Rev. Biophys. Chem. , vol.17 , pp. 145-166
    • Johnson Jr., W.C.1
  • 21
    • 0003752593 scopus 로고
    • Potato protein concentrates: The influence of various methods of recovery upon yield, compositional and functional characteristics
    • Knorr, D.; Kohler, G. O.; Betschart, A. A. Potato protein concentrates: the influence of various methods of recovery upon yield, compositional and functional characteristics. J. Food Process. Preserv. 1977, 1, 235-247.
    • (1977) J. Food Process. Preserv. , vol.1 , pp. 235-247
    • Knorr, D.1    Kohler, G.O.2    Betschart, A.A.3
  • 24
    • 0015882223 scopus 로고
    • The equilibrium unfolding parameters of horse and sperm whale myoglobulin
    • Puett, D. The equilibrium unfolding parameters of horse and sperm whale myoglobulin. J. Biol. Chem. 1973, 248, 4623-4634.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4623-4634
    • Puett, D.1
  • 25
    • 84986435891 scopus 로고
    • Patatin and esterase in Desiree potato tubers
    • Racusen, D. Patatin and esterase in Desiree potato tubers J. Pood Biochem. 1985, 9, 361-167.
    • (1985) J. Pood Biochem. , vol.9 , pp. 361-1167
    • Racusen, D.1
  • 26
    • 84986514841 scopus 로고
    • A major soluble glycoprotein of potato tubers
    • Racusen, D.; Foote, M. A major soluble glycoprotein of potato tubers. J. Food Biochem. 1980, 4, 43-52.
    • (1980) J. Food Biochem. , vol.4 , pp. 43-52
    • Racusen, D.1    Foote, M.2
  • 27
    • 84986468716 scopus 로고
    • Molecular weight of palatin, a major potato tuber protein
    • Racusen, D.; Weller, D. L. Molecular weight of palatin, a major potato tuber protein. J. Food Biochem. 1984, 8, 103-107.
    • (1984) J. Food Biochem. , vol.8 , pp. 103-107
    • Racusen, D.1    Weller, D.L.2
  • 28
    • 0347760574 scopus 로고
    • Isolation and characterization of a gene from Solanum tuberosum encoding patatin, the major storage protein of potato tubers
    • Rosahl, S.; Schmidt, R.; Schnell, J.; Willmitzer, L. Isolation and characterization of a gene from Solanum tuberosum encoding patatin, the major storage protein of potato tubers. Mol. Gen. Genet. 1986, 203, 214-220.
    • (1986) Mol. Gen. Genet. , vol.203 , pp. 214-220
    • Rosahl, S.1    Schmidt, R.2    Schnell, J.3    Willmitzer, L.4
  • 29
    • 0030586763 scopus 로고    scopus 로고
    • Characterization of a molten globule intermediate during GdnHCl-induced unfolding of RTEM α-lactamase from Escherichia coli
    • Sarkar, D.; DasGupta, C. Characterization of a molten globule intermediate during GdnHCl-induced unfolding of RTEM α-lactamase from Escherichia coli. Biochim. Biophys. Acta 1996, 1296, 85-94.
    • (1996) Biochim. Biophys. Acta , vol.1296 , pp. 85-94
    • Sarkar, D.1    DasGupta, C.2
  • 30
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformaitonal change
    • Creighton, T. E., Ed.; IRL Press: Oxford
    • Schmid, F. X. Spectral methods of characterizing protein conformation and conformaitonal change. In Protein Structure: A practical approach; Creighton, T. E., Ed.; IRL Press: Oxford, 1989.
    • (1989) Protein Structure: A Practical Approach
    • Schmid, F.X.1
  • 31
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1'-bis(anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • Shi, L.; Palleros, P. R.; Fink, A. L. Protein conformational changes induced by 1,1'-bis(anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK. Biochemistry 1994, 33, 7536-7546.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, P.R.2    Fink, A.L.3
  • 32
    • 0000816824 scopus 로고
    • Targeting and glycosylation of patatin, the major potato tuber protein in leaves of transgenic tobacco
    • Sonnewald, U.; Sturm, A.; Chrispeels, M. J.; Willmitzer, L. Targeting and glycosylation of patatin, the major potato tuber protein in leaves of transgenic tobacco. Planta 1989, 179, 171-180.
    • (1989) Planta , vol.179 , pp. 171-180
    • Sonnewald, U.1    Sturm, A.2    Chrispeels, M.J.3    Willmitzer, L.4
  • 35
    • 0029148319 scopus 로고
    • Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis
    • van Stokkum, I. H. M.; Linsdell, H.; Hadden, J. M.; Haris, P. I.; Chapman, D.; Bloemendal, M. Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis. Biochemistry 1995, 34, 10508-10518.
    • (1995) Biochemistry , vol.34 , pp. 10508-10518
    • Van Stokkum, I.H.M.1    Linsdell, H.2    Hadden, J.M.3    Haris, P.I.4    Chapman, D.5    Bloemendal, M.6
  • 36
    • 0028284743 scopus 로고
    • The thermal unfolding of bovine α-lactalbumin
    • Vanderheeren, G.; Hanssens, I. The thermal unfolding of bovine α-lactalbumin. J. Biol. Chem. 1994, 269, 7090-7094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7090-7094
    • Vanderheeren, G.1    Hanssens, I.2
  • 37
    • 0027527209 scopus 로고
    • Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side-chains
    • Vuilleumier, S.; Sancho, J.; Loewenthal, R.; Fersht, A. D. Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side-chains. Biochemistry 1993, 32, 10303-10313.
    • (1993) Biochemistry , vol.32 , pp. 10303-10313
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.D.4
  • 38
    • 0027199523 scopus 로고
    • Effect of pH and denaturants on the folding and stability of murine interleukin-6
    • Ward, L. D.; Zhang, J. G.; Checkley, G.; Preston, B.; Simpson, R. J. Effect of pH and denaturants on the folding and stability of murine interleukin-6. Protein Sci. 1993, 2, 1291-1300.
    • (1993) Protein Sci. , vol.2 , pp. 1291-1300
    • Ward, L.D.1    Zhang, J.G.2    Checkley, G.3    Preston, B.4    Simpson, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.