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The sarcoplasmic reticulum Ca2+-ATPase.

作者信息

Møller J V, Andersen J P, le Maire M

出版信息

Mol Cell Biochem. 1982 Feb 5;42(2):83-107. doi: 10.1007/BF00222696.

DOI:10.1007/BF00222696
PMID:6278286
Abstract
摘要

相似文献

1
The sarcoplasmic reticulum Ca2+-ATPase.肌浆网Ca2+ -ATP酶
Mol Cell Biochem. 1982 Feb 5;42(2):83-107. doi: 10.1007/BF00222696.
2
Ion pathways in proteins of the sarcoplasmic reticulum.肌浆网蛋白质中的离子通道
Ann N Y Acad Sci. 1980;358:138-48. doi: 10.1111/j.1749-6632.1980.tb15392.x.
3
Characterization of partial reactions in the catalytic and transport cycle of sarcoplasmic reticulum ATPase.
Soc Gen Physiol Ser. 1987;41:231-55.
4
The separate profile structures of the functional calcium pump protein and the phospholipid bilayer within isolated sarcoplasmic reticulum membranes determined by X-ray and neutron diffraction.通过X射线和中子衍射确定的分离的肌浆网细胞膜内功能性钙泵蛋白和磷脂双层的轮廓结构。
Biochim Biophys Acta. 1985 Jul 11;817(1):103-22. doi: 10.1016/0005-2736(85)90073-2.
5
The pH dependence of the Ca2+, Mg2+-ATPase of sarcoplasmic reticulum: evidence that the Ca2+ translocator bears a doubly negative charge.肌浆网Ca2+、Mg2+-ATP酶的pH依赖性：Ca2+转运体带有双负电荷的证据。
J Membr Biol. 1983;74(1):25-40. doi: 10.1007/BF01870592.
6
Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum.肌浆球蛋白可使骨骼肌肌浆网中Ca2+-ATP酶将ATP水解与Ca2+蓄积的过程解偶联。
Biochem J. 2002 Jan 15;361(Pt 2):277-86. doi: 10.1042/0264-6021:3610277.
7
Thermodynamic analysis of muscle ATPase mechanisms.
Physiol Rev. 1985 Apr;65(2):467-551. doi: 10.1152/physrev.1985.65.2.467.
8
Effect of lipid composition on the calcium/adenosine 5'-triphosphate coupling ratio of the Ca2+-ATPase of sarcoplasmic reticulum.脂质组成对肌浆网Ca2+-ATP酶钙/三磷酸腺苷偶联率的影响。
Biochemistry. 1984 Jan 3;23(1):130-5. doi: 10.1021/bi00296a021.
9
Mechanisms of Ca2+ release from sarcoplasmic reticulum of skeletal muscle.骨骼肌肌浆网中Ca2+释放的机制。
Physiol Rev. 1984 Oct;64(4):1240-320. doi: 10.1152/physrev.1984.64.4.1240.
10
Twenty questions concerning the reaction cycle of the sarcoplasmic reticulum calcium pump.关于肌浆网钙泵反应循环的二十个问题。
CRC Crit Rev Biochem. 1984;17(2):123-51. doi: 10.3109/10409238409113603.

引用本文的文献

1
Monovalent ion and calcium ion fluxes in sarcoplasmic reticulum.肌浆网中的单价离子和钙离子通量
Mol Cell Biochem. 1983;55(1):65-82. doi: 10.1007/BF00229243.
2
Crystallization of intramembrane particles in rabbit sarcoplasmic reticulum vesicles by vanadate.钒酸盐诱导兔肌浆网囊泡内膜颗粒结晶
J Muscle Res Cell Motil. 1984 Aug;5(4):431-42. doi: 10.1007/BF00818261.
3
Monomeric solubilized sarcoplasmic reticulum Ca pump protein: demonstration of Ca binding and dissociation coupled to ATP hydrolysis.单体溶解的肌浆网钙泵蛋白：钙结合和解离与ATP水解偶联的证明。

本文引用的文献

1
Variable Ca2+ transport:phosphoprotein ratios in the early part of the GTP-driven calcium-transport reaction of the sarcoplasmic reticulum.
Eur J Biochem. 1981 Jan;113(3):611-6. doi: 10.1111/j.1432-1033.1981.tb05106.x.
2
Recent developments in solution x-ray scattering.
Annu Rev Biophys Bioeng. 1980;9:1-29. doi: 10.1146/annurev.bb.09.060180.000245.
3
Chopping and changing in immunoglobulin genes.免疫球蛋白基因的频繁改变。
Nature. 1980 Oct 2;287(5781):390-2. doi: 10.1038/287390a0.
4
Proc Natl Acad Sci U S A. 1984 Nov;81(21):6623-6. doi: 10.1073/pnas.81.21.6623.
4
Oligomeric structure and the anion transport function of human erythrocyte band 3 protein.人红细胞带3蛋白的寡聚体结构与阴离子转运功能
J Membr Biol. 1984;80(2):105-17. doi: 10.1007/BF01868768.
5
Direct demonstration of structural changes in soluble, monomeric Ca2+-ATPase associated with Ca2+ release during the transport cycle.在转运循环中与钙离子释放相关的可溶性单体钙ATP酶结构变化的直接证明。
Proc Natl Acad Sci U S A. 1985 Jul;82(14):4573-7. doi: 10.1073/pnas.82.14.4573.
6
Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins.钠钾泵和钙泵蛋白中E1-E2构象转变的结构基础。
J Membr Biol. 1988 Jul;103(2):95-120. doi: 10.1007/BF01870942.
7
Phospholamban stoichiometry in canine cardiac muscle sarcoplasmic reticulum.
Neurochem Res. 1987 Oct;12(10):937-41. doi: 10.1007/BF00966316.
8
Fluorescence energy transfer as an indicator of Ca2+-ATPase interactions in sarcoplasmic reticulum.荧光能量转移作为肌浆网中Ca2 + -ATP酶相互作用的指标。
Biophys J. 1987 Feb;51(2):205-20. doi: 10.1016/S0006-3495(87)83326-X.
9
Localization of E1-E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling.通过胰蛋白酶切割和疏水标记定位肌浆网钙ATP酶的E1-E2构象转变
J Membr Biol. 1986;93(1):85-92. doi: 10.1007/BF01871021.
10
The reaction of N-(1-pyrene)maleimide with sarcoplasmic reticulum.N-（1-芘基）马来酰亚胺与肌浆网的反应
Biophys J. 1986 Feb;49(2):411-24. doi: 10.1016/S0006-3495(86)83651-7.
Freeze-fracture study of water-soluble, standard proteins and of detergent-solubilized forms of sarcoplasmic reticulum Ca2+-ATPase.
Biochim Biophys Acta. 1981 Apr 22;643(1):115-25. doi: 10.1016/0005-2736(81)90223-6.
5
Preparative isolation of Apo(Ca2+-ATPase) from sarcoplasmic reticulum and the reactivation by lysophosphatidylcholine of Ca2+-dependent ATP hydrolysis and partial-reaction steps of the enzyme.
Eur J Biochem. 1981 Feb;114(2):339-47. doi: 10.1111/j.1432-1033.1981.tb05153.x.
6
The modulation of Ca2+-ATPase activity of sarcoplasmic reticulum by membrane cholesterol. The effect of enzyme coupling.膜胆固醇对肌浆网Ca2+-ATP酶活性的调节。酶偶联的作用。
Biochim Biophys Acta. 1981 Feb 20;641(1):265-9. doi: 10.1016/0005-2736(81)90590-3.
7
The dependence for reactivation of lipid-depleted Ca2+-ATPase of sarcoplasmic reticulum by non-ionic detergents on their hydrophile/lipophile balance.
FEBS Lett. 1980 Dec 1;121(2):235-8. doi: 10.1016/0014-5793(80)80350-4.
8
Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein.用荧光素选择性标记的肌浆网Ca2+ -ATP酶的寡聚体结构及构象变化的指征。
Biochim Biophys Acta. 1980 Nov 20;626(1):255-61. doi: 10.1016/0005-2795(80)90216-0.
9
Studies on the structure of the calcium-dependent adenosine triphosphatase from rabbit skeletal muscle sarcoplasmic reticulum.
Arch Biochem Biophys. 1980 Sep;203(2):780-91. doi: 10.1016/0003-9861(80)90239-8.
10
Protein rotational diffusion and lipid structure of reconstituted systems of Ca2+-activated adenosine triphosphatase.
J Mol Biol. 1980 Aug 5;141(2):119-32. doi: 10.1016/0022-2836(80)90380-0.