Rotational mobility of Ca2+-ATPase of sarcoplasmic reticulum in viscous media

被引:2
|
作者
Torok, M
Jakab, G
Berczi, A
Dux, L
Horvath, LI
机构
[1] BIOL RES CTR, INST BIOPHYS, H-6701 SZEGED, HUNGARY
[2] SZENT GYORGYI ALBERT MED SCH, DEPT BIOCHEM, SZEGED, HUNGARY
来源
基金
匈牙利科学研究基金会;
关键词
rotational mobility; Ca2+-ATPase; saturation transfer ESR; viscosity dependence;
D O I
10.1016/S0005-2736(97)00021-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The rotational diffusion of Ca2+-ATPase [Ca2+,Mg2+-activated ATP phosphohydrolase E.C. 3.6.1.38] was studied in native sarcoplasmic reticulum membrane by saturation transfer ESR spectroscopy after covalent labelling of intramembranous sulfhydryl groups with nitroxyl derivative of maleimide (5-MSL) as a function of sucrose and glycerol in the suspending medium. The relative enzymatic activity of sarcoplasmic reticulum was followed by increasing the viscosity of the aqueous phase. The ATP hydrolysing activity of the enzyme decreased differently on adding sucrose and glycerol. In the case of sucrose the reciprocal of power dependence of viscosity was observed, whereas for glycerol an exponential decay law was obtained, indicating solvent-protein interaction. On increasing the viscosity of the aqueous phase by either sucrose or glycerol, no changes were observed in the intramembranous viscosity as measured using intercalated spin-labelled stearic acid (16-SASL). The effective rotational correlation time of the protein was measured, as a mobility parameter, using saturation transfer ESR spectroscopy and found to be increased linearly with the viscosity of the sucrose containing medium and for the extramembranous size a height of 6.8 nm was obtained, indicating that approx. 82% of the volume of Ca2+-ATPase protein is external to the sarcoplasmic reticulum. The addition of glycerol probably promoted protein-protein interaction, as indicated by the larger changes in rotational diffusion and non-linear viscosity dependence.
引用
收藏
页码:193 / 200
页数:8
相关论文
共 50 条
  • [21] The oxidative inactivation of sarcoplasmic reticulum Ca2+-ATPase by peroxynitrite
    Viner, RI
    Huhmer, AFR
    Bigelow, DJ
    Schoneich, C
    FREE RADICAL RESEARCH, 1996, 24 (04) : 243 - 259
  • [22] Activation of the sarcoplasmic reticulum Ca2+-ATPase induced by exercise
    Ferrington, DA
    Reijneveld, JC
    Bar, PR
    Bigelow, DJ
    BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1996, 1279 (02): : 203 - 213
  • [23] Effect of halothane on the oligomerization of the sarcoplasmic reticulum Ca2+-ATPase
    Brennan, LK
    Froemming, GR
    Ohlendieck, K
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 271 (03) : 770 - 776
  • [24] ROTATIONAL MOBILITY OF CA2+-MG2+-DEPENDENT ATPASE OF SARCOPLASMIC-RETICULUM
    BURKLI, A
    CHERRY, RJ
    EXPERIENTIA, 1978, 34 (07): : 907 - 907
  • [25] Ca2+ occlusion of sarcoplasmic reticulum Ca2+-ATPase by CrATP
    Juul, BS
    Moller, JV
    NA,K-ATPASE AND RELATED CATION PUMPS: STRUCTURE, FUNCTION, AND REGULATORY MECHANISMS, 2003, 986 : 318 - 319
  • [26] Mn2+ transport by Ca2+-ATPase of sarcoplasmic reticulum
    Yonekura, Shin-Ichiro
    Toyoshima, Chikashi
    FEBS LETTERS, 2016, 590 (14): : 2086 - 2095
  • [27] Effect of the local anesthetic carticaine on the sarcoplasmic reticulum Ca2+-ATPase
    Takara, D
    Sánchez, GA
    Yoshida, CA
    Alonso, GL
    NA/K-ATPASE AND RELATED ATPASES, 2000, 1207 : 751 - 754
  • [28] Structural basis of ion pumping by CA2+-ATpase of the sarcoplasmic reticulum
    Toyoshima, C
    Inesi, G
    ANNUAL REVIEW OF BIOCHEMISTRY, 2004, 73 : 269 - 292
  • [29] Structural basis of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum
    Toyoshima, C
    Nomura, H
    Sugita, Y
    FEBS LETTERS, 2003, 555 (01): : 106 - 110
  • [30] Is the Ca2+-ATPase from sarcoplasmic reticulum also a heat pump?
    Signe Kjelstrup
    Leopoldo de Meis
    Dick Bedeaux
    Jean-Marc Simon
    European Biophysics Journal, 2008, 38 : 59 - 67