(Q39861054)

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Enzymatically active Ca2+ ATPase from sarcoplasmic reticulum membranes, solubilized by nonionic detergents. Role of lipid for aggregation of the protein

scientific article published on October 10, 1978

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scholarly article

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Europe PubMed Central

15 September 2017

Enzymatically active Ca2+ ATPase from sarcoplasmic reticulum membranes, solubilized by nonionic detergents. Role of lipid for aggregation of the protein (English)

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10.1016/S0021-9258(17)38028-6

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12 May 2022

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16 December 2022

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16 December 2022

calcium-transporting ATPases

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16 December 2022

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10.1016/S0021-9258(17)38028-6

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16 December 2022

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16 December 2022

author name string

M. L. Maire

1

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12 May 2022

K. E. Lind

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K. E. Jørgensen

3

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16 December 2022

H. Røigaard

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16 December 2022

J. V. Møller

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publication date

1 October 1978

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15 September 2017

10 October 1978

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16 December 2022

number of pages

10

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full work available at URL

http://intl.jbc.org/cgi/content/abstract/253/19/7051

online access status

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16 December 2022

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10.1016/S0021-9258(17)38028-6

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16 December 2022

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10.1016/S0021-9258(17)38028-6

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16 December 2022

Journal of Biological Chemistry

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15 September 2017

253

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15 September 2017

19

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Europe PubMed Central

15 September 2017

7051-7060

1 reference

Europe PubMed Central

15 September 2017

The binding of nucleotides and bivalent cations to the calcium-and-magnesium ion-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum

1

1 reference

10.1016/S0021-9258(17)38028-6

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The mechanism of ATP hydrolysis by sarcoplasmic reticulum

2

1 reference

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Assembly of ATPase protein in sarcoplasmic reticulum membranes

5

1 reference

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Fluorescence energy transfer between Ca2+transport ATPase molecules in artificial membranes

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Cross-linking of the sarcoplasmic reticulum ATPase protein

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What is the Phospholipid Specificity of a Reconstituted Calcium Pump?

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Properties of deoxycholate solubilized sarcoplasmic reticulum Ca2+ ion-dependent ATPase

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The functional unit of calcium-plus-magnesium-ion-dependent adenosine triphosphatase from sarcoplasmic reticulum. The aggregational state of the deoxycholate-solubilized protein in an enzymically active form

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Solubilization of sarcoplasmic reticulum with Triton X-100

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The separation of the solubilized proteins of the sarcoplasmic reticulum on DEAE-cellulose and its modification

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Properties of the calcium-independent ATPase of the membranes of the sarcoplasmic reticulum delipidated by the nonionic detergent Triton X-100

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Retention of enzyme activity by detergent-solubilized sarcoplasmic Ca2+ion-activated ATPase

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Isolation of sarcoplasmic reticulum by zonal centrifugation and purification of Ca 2+ -pump and Ca 2+ -binding proteins

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Reaction of sarcoplasmic reticulum Ca2+-ATPase in different functional states with 5.5′-dithiobis(2-nitrobenzoate)

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Measurement of protein-binding phenomena by gel filtration

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Erythrocyte spectrin. Purification in deoxycholate and preliminary characterization

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The effect of delipidation on the adenosine triphosphatase of sarcoplasmic reticulum. Electron microscopy and physical properties

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Europe PubMed Central

15 September 2017

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