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1
The E1----E2 transition of Ca2+-transporting ATPase in sarcoplasmic reticulum occurs without major changes in secondary structure. A circular-dichroism study.肌浆网中钙离子转运ATP酶从E1到E2的转变过程中,二级结构未发生重大变化。一项圆二色性研究。
Biochem J. 1987 Feb 1;241(3):663-9. doi: 10.1042/bj2410663.
2
Infrared spectroscopic characterization of the structural changes connected with the E1----E2 transition in the Ca2+-ATPase of sarcoplasmic reticulum.肌质网Ca2+-ATP酶中与E1----E2转变相关的结构变化的红外光谱表征。
J Biol Chem. 1987 Jul 5;262(19):9037-43.
3
The effect of high pressure on the conformation, interactions and activity of the Ca(2+)-ATPase of sarcoplasmic reticulum.高压对肌浆网Ca(2+)-ATP酶的构象、相互作用及活性的影响
Biochim Biophys Acta. 1991 Dec 9;1070(2):355-73. doi: 10.1016/0005-2736(91)90077-l.
4
The effects of membrane potential and lanthanides on the conformation of the Ca2+-transport ATPase in sarcoplasmic reticulum.膜电位和镧系元素对肌浆网中Ca2+转运ATP酶构象的影响。
Biochem J. 1986 Mar 1;234(2):363-71. doi: 10.1042/bj2340363.
5
The interaction of vanadate ions with the Ca-ATPase from sarcoplasmic reticulum.钒酸盐离子与肌浆网钙ATP酶的相互作用。
J Biol Chem. 1982 Jun 10;257(11):6111-9.
6
Vanadate inhibition of the Ca2+-dependent conformational change of the sarcoplasmic reticulum Ca2+-ATPase.钒酸盐对肌浆网Ca2+-ATP酶Ca2+依赖性构象变化的抑制作用。
FEBS Lett. 1982 Mar 22;139(2):237-40. doi: 10.1016/0014-5793(82)80860-0.
7
Pressure effects on sarcoplasmic reticulum.压力对肌浆网的影响。
J Biol Chem. 1986 Oct 25;261(30):13943-56.
8
Competition between decavanadate and fluorescein isothiocyanate on the Ca2+-ATPase of sarcoplasmic reticulum.十钒酸盐与异硫氰酸荧光素对肌浆网Ca2+-ATP酶的竞争作用
Eur J Biochem. 1985 Aug 1;150(3):455-60. doi: 10.1111/j.1432-1033.1985.tb09043.x.
9
Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum.化学修饰对肌浆网中Ca2+-ATP酶结晶的影响。
Biochim Biophys Acta. 1987 Jan 26;896(2):187-95. doi: 10.1016/0005-2736(87)90179-9.
10
Conformational transitions in the Ca2+ + Mg2+-activated ATPase and the binding of Ca2+ ions.Ca2+ + Mg2+激活的ATP酶中的构象转变以及Ca2+离子的结合
Biochem J. 1986 Jul 1;237(1):197-206. doi: 10.1042/bj2370197.

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1
Isolation of the Sarcoplasmic Reticulum Ca-ATPase from Rabbit Fast-Twitch Muscle.从兔快肌中分离肌浆网钙-ATP酶
Methods Protoc. 2023 Oct 19;6(5):102. doi: 10.3390/mps6050102.
2
Structure of the Ca2+ pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9-A resolution.肌浆网Ca2+泵的结构:以9埃分辨率沿脂质双层观察。
Biophys J. 1998 Jul;75(1):41-52. doi: 10.1016/S0006-3495(98)77493-4.
3
Preservation of the native structure and function of Ca2+-ATPase from sarcoplasmic reticulum: solubilization and reconstitution by new short-chain phospholipid detergent 1,2-diheptanoyl-sn-phosphatidylcholine.肌浆网中Ca2+ -ATP酶天然结构和功能的保存:新型短链磷脂去污剂1,2 -二庚酰 -sn -磷脂酰胆碱的增溶和重组
Biochem J. 1997 Jul 15;325 ( Pt 2)(Pt 2):533-42. doi: 10.1042/bj3250533.
4
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.

本文引用的文献

1
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
2
Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism.利用真空紫外圆二色性测定溶液中蛋白质的二级结构。
J Mol Biol. 1980 Apr;138(2):149-78. doi: 10.1016/0022-2836(80)90282-x.
3
Circular dichroism analyses of membrane proteins: an examination of differential light scattering and absorption flattening effects in large membrane vesicles and membrane sheets.膜蛋白的圆二色性分析:对大膜泡和膜片层中差分光散射和吸收平坦化效应的研究。
Anal Biochem. 1984 Nov 1;142(2):317-28. doi: 10.1016/0003-2697(84)90471-8.
4
Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles.在小单层囊泡的圆二色光谱中,差分光散射和吸收平坦化光学效应极小。
Biochemistry. 1984 Jun 5;23(12):2667-73. doi: 10.1021/bi00307a020.
5
Structure and function of the calcium pump protein of sarcoplasmic reticulum.肌浆网钙泵蛋白的结构与功能
Annu Rev Physiol. 1982;44:297-317. doi: 10.1146/annurev.ph.44.030182.001501.
6
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.
7
Secondary structural composition of the Na/K-ATPase E1 and E2 conformers.钠钾ATP酶E1和E2构象体的二级结构组成
J Biol Chem. 1984 Feb 25;259(4):2622-8.
8
Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles.线粒体质子腺苷三磷酸酶蛋白脂质通道在磷脂囊泡中的折叠。
Biochemistry. 1982 Sep 28;21(20):4960-8. doi: 10.1021/bi00263a020.
9
Simple model for the chemical potential change of a transported ion in active transport.主动运输中转运离子化学势变化的简单模型。
Proc Natl Acad Sci U S A. 1982 May;79(9):2882-4. doi: 10.1073/pnas.79.9.2882.
10
Membrane crystals of Ca2+-ATPase in sarcoplasmic reticulum of fast and slow skeletal and cardiac muscles.快、慢骨骼肌及心肌肌浆网中Ca2+ -ATP酶的膜晶体
Eur J Biochem. 1984 May 15;141(1):43-9. doi: 10.1111/j.1432-1033.1984.tb08154.x.

肌浆网中钙离子转运ATP酶从E1到E2的转变过程中,二级结构未发生重大变化。一项圆二色性研究。

The E1----E2 transition of Ca2+-transporting ATPase in sarcoplasmic reticulum occurs without major changes in secondary structure. A circular-dichroism study.

作者信息

Csermely P, Katopis C, Wallace B A, Martonosi A

出版信息

Biochem J. 1987 Feb 1;241(3):663-9. doi: 10.1042/bj2410663.

DOI:10.1042/bj2410663
PMID:2954535
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1147615/
Abstract

C.d. spectroscopy was used to investigate the structures of Ca2+-ATPase (Ca2+-transporting ATPase) in the E1 and E2 states in native, in fluorescein isothiocyanate (FITC)-labelled and in solubilized sarcoplasmic reticulum (SR) preparations. The E1 state was stabilized by 100 microM-Ca2+ and the E2 state by 0.5 mM-Na3 VO4 and 0.1 mM-EGTA. There were no significant differences detected in the c.d. spectra and the calculated secondary structures between the E1 and E2 states in any of the three types of preparations. The FITC-labelled SR did show the characteristic changes in FITC fluorescence on addition of Ca2+ or vanadate, indicating that the preparation was competent for E1----E2 transitions. Therefore the absence of changes in the c.d. spectra implies that the E1----E2 transition in the Ca2+-ATPase does not involve a major net rearrangement of the polypeptide backbone conformation.

摘要

利用圆二色光谱法研究了天然的、异硫氰酸荧光素(FITC)标记的以及溶解的肌浆网(SR)制剂中处于E1和E2状态的Ca2 + -ATP酶(Ca2 +转运ATP酶)的结构。通过100微摩尔/升的Ca2 +使E1状态稳定,通过0.5毫摩尔/升的Na3VO4和0.1毫摩尔/升的乙二醇双四乙酸(EGTA)使E2状态稳定。在这三种制剂中的任何一种中,E1和E2状态之间的圆二色光谱以及计算出的二级结构均未检测到显著差异。添加Ca2 +或钒酸盐后,FITC标记的肌浆网确实显示出FITC荧光的特征性变化,表明该制剂能够进行E1→E2转变。因此,圆二色光谱没有变化意味着Ca2 + -ATP酶中的E1→E2转变不涉及多肽主链构象的重大净重排。