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Volumn 209, Issue 1-2, 2000, Pages 105-112

Thermal analysis of the plasma membrane Ca2+ATPase

Author keywords

Ca2+ ATPase; Calcium; Cholesterol; Thermal analysis

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM; CHOLESTEROL;

EID: 0033921693     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1007182907274     Document Type: Article
Times cited : (10)

References (37)
  • 1
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • Carafoli E: Intracellular calcium homeostasis. Ann Rev Biochem 56: 395-433, 1987
    • (1987) Ann Rev Biochem , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 3
    • 0028113894 scopus 로고
    • Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli E: Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J 8: 993-1002, 1994
    • (1994) FASEB J , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 4
    • 0020331649 scopus 로고
    • 2+ pumping ATPase of plasma membranes. Purification, reconstitution and properties
    • 2+ pumping ATPase of plasma membranes. Purification, reconstitution and properties. Biochim Biophys Acta 683: 279-301, 1982
    • (1982) Biochim Biophys Acta , vol.683 , pp. 279-301
    • Carafoli, E.1    Zurini, M.2
  • 6
    • 0022979031 scopus 로고
    • Direct Regulatory Effect of Cholesterol on the Calmodulin Stimulated Calcium Pump of Cardiac Sarcolemma
    • Ortega A, Mas-Oliva J: Direct Regulatory Effect of Cholesterol on the Calmodulin Stimulated Calcium Pump of Cardiac Sarcolemma. Biochem Biophys Res Commun 139: 868-874, 1986
    • (1986) Biochem Biophys Res Commun , vol.139 , pp. 868-874
    • Ortega, A.1    Mas-Oliva, J.2
  • 9
    • 0023098022 scopus 로고
    • Protection of the membrane calcium adenosine triphosphatase by cholesterol from thermal inactivation
    • Cheng K-H, Hui SW, Lepock JR: Protection of the membrane calcium adenosine triphosphatase by cholesterol from thermal inactivation. Cancer Res 47: 1255-1262, 1987
    • (1987) Cancer Res , vol.47 , pp. 1255-1262
    • Cheng, K.-H.1    Hui, S.W.2    Lepock, J.R.3
  • 10
    • 0024457025 scopus 로고
    • Cholesterol stabilizes the structure of the nicotinic acetylcholine receptor reconstituted in lipid vesicles
    • Artigues A, Villar MT, Fernandez J, Farragut JA, Gonzalez-Ros JM: Cholesterol stabilizes the structure of the nicotinic acetylcholine receptor reconstituted in lipid vesicles. Biochim Biophys Acta 985: 325-330, 1989
    • (1989) Biochim Biophys Acta , vol.985 , pp. 325-330
    • Artigues, A.1    Villar, M.T.2    Fernandez, J.3    Farragut, J.A.4    Gonzalez-Ros, J.M.5
  • 11
    • 0025730412 scopus 로고
    • Effects of cholesterol on the function and thermotropic properties of pure UDP-glucuronosyltransferase
    • Rotenberg M, Zakim D: Effects of cholesterol on the function and thermotropic properties of pure UDP-glucuronosyltransferase. J Biol Chem 266: 4159-4161, 1991
    • (1991) J Biol Chem , vol.266 , pp. 4159-4161
    • Rotenberg, M.1    Zakim, D.2
  • 13
    • 0025129186 scopus 로고
    • Thermal stability of membrane-reconstituted yeast cytochrome c oxidase
    • Morin PE, Diggs D, Freire E: Thermal stability of membrane-reconstituted yeast cytochrome c oxidase. Biochemistry 29: 781-788, 1990
    • (1990) Biochemistry , vol.29 , pp. 781-788
    • Morin, P.E.1    Diggs, D.2    Freire, E.3
  • 14
    • 0023653192 scopus 로고
    • Differential detergent solubility investigation of thermally induced transitions in cytochrome c oxidase
    • Rigell CW, Freire E: Differential detergent solubility investigation of thermally induced transitions in cytochrome c oxidase. Biochemistry 26: 4366-4371, 1987
    • (1987) Biochemistry , vol.26 , pp. 4366-4371
    • Rigell, C.W.1    Freire, E.2
  • 16
    • 0028104344 scopus 로고
    • Divalent cations stabilize the conformation of plasma cell membrane glycoprotein Pc-1 (alkaline phosphodiesterase I)
    • Belli SI, Sali A, Goding JW: Divalent cations stabilize the conformation of plasma cell membrane glycoprotein Pc-1 (alkaline phosphodiesterase I). Biochem J 304: 75-80, 1994
    • (1994) Biochem J , vol.304 , pp. 75-80
    • Belli, S.I.1    Sali, A.2    Goding, J.W.3
  • 18
    • 0028271963 scopus 로고
    • Cation binding to a Bacillus (1,3-1,4)-beta glucanase. Geometry, affinity and effect on protein stability
    • Keitel T, Meldgaard M, Heinemann U: Cation binding to a Bacillus (1,3-1,4)-beta glucanase. Geometry, affinity and effect on protein stability. Bur J Biochem 222: 203-214, 1994
    • (1994) Bur J Biochem , vol.222 , pp. 203-214
    • Keitel, T.1    Meldgaard, M.2    Heinemann, U.3
  • 21
    • 0026683468 scopus 로고
    • Entropic stabilization of a mutant human lysozyme induced by calcium binding
    • Kuroki R, Kawakita S, Nakamura H, Yutani K: Entropic stabilization of a mutant human lysozyme induced by calcium binding. Proc Natl Acad Sci USA 89: 6803-6807, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6803-6807
    • Kuroki, R.1    Kawakita, S.2    Nakamura, H.3    Yutani, K.4
  • 22
    • 0023862963 scopus 로고
    • Differential scanning calorimetry of Cu, Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives
    • Roe JA, Butler A, Scholler DM, Valentine JS, Marky L, Breslauer KJ: Differential scanning calorimetry of Cu, Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives. Biochemistry 27: 950-958, 1988
    • (1988) Biochemistry , vol.27 , pp. 950-958
    • Roe, J.A.1    Butler, A.2    Scholler, D.M.3    Valentine, J.S.4    Marky, L.5    Breslauer, K.J.6
  • 23
    • 0018786919 scopus 로고
    • Calorimetry of alkaline phosphatase stability of the monomer and effect of metal ion and phosphate binding on dimer stability
    • Chlebowski JF, Mabrey S, Falk MC: Calorimetry of alkaline phosphatase stability of the monomer and effect of metal ion and phosphate binding on dimer stability. J Biol Chem 254: 5745-5753, 1979
    • (1979) J Biol Chem , vol.254 , pp. 5745-5753
    • Chlebowski, J.F.1    Mabrey, S.2    Falk, M.C.3
  • 24
    • 0026646104 scopus 로고
    • Thermostability and activation by divalent cations of the membrane-bound inorganic pyrophosphatase of Rhodospirillum rubrum
    • Ordaz H, Sosa A, Romero I, Celis H: Thermostability and activation by divalent cations of the membrane-bound inorganic pyrophosphatase of Rhodospirillum rubrum. Int J Biochem 24: 1633-1638, 1992
    • (1992) Int J Biochem , vol.24 , pp. 1633-1638
    • Ordaz, H.1    Sosa, A.2    Romero, I.3    Celis, H.4
  • 26
    • 0030690394 scopus 로고    scopus 로고
    • Protein stability: Still an unsolved problem
    • Richards FM: Protein stability: Still an unsolved problem. Cell Mol Life Sci 53: 790-802, 1997
    • (1997) Cell Mol Life Sci , vol.53 , pp. 790-802
    • Richards, F.M.1
  • 27
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational characteristics related to thermostability
    • Querol E, Perez-Pons JA, Mozo-Villarias A: Analysis of protein conformational characteristics related to thermostability. Prot Eng 9: 265-271, 1996
    • (1996) Prot Eng , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 28
    • 0019327184 scopus 로고
    • Isolation of seales vesicles highly enriched with sarcolemma markers from canine ventricle
    • Alstyne E van, Burk R, Knickelbein R, Hungerford R, et al: Isolation of seales vesicles highly enriched with sarcolemma markers from canine ventricle. Biochim Biophys Acta 602: 131-143, 1980
    • (1980) Biochim Biophys Acta , vol.602 , pp. 131-143
    • Van Alstyne, E.1    Burk, R.2    Knickelbein, R.3    Hungerford, R.4
  • 33
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing metals and ligands
    • Fabiato A: Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing metals and ligands. Meth Enzymol 157: 378-416, 1988
    • (1988) Meth Enzymol , vol.157 , pp. 378-416
    • Fabiato, A.1
  • 34
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensandoun A, Wenstein D: Assay of proteins in the presence of interfering materials. Anal Biochem 70: 241-250, 1976
    • (1976) Anal Biochem , vol.70 , pp. 241-250
    • Bensandoun, A.1    Wenstein, D.2
  • 36
    • 0022587646 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum. FEBS Lett 194: 258-262, 1986
    • (1986) FEBS Lett , vol.194 , pp. 258-262
    • Nakamoto, R.K.1    Inesi, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.