Characterisation of thapsigargin-releasable Ca(2+) from the Ca(2+)-ATPase of sarcoplasmic reticulum at limiting [Ca(2+)]. (Q46501707)

22 December 2017

title

Characterisation of thapsigargin-releasable Ca(2+) from the Ca(2+)-ATPase of sarcoplasmic reticulum at limiting [Ca(2+)]. (English)

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22 December 2017

author name string

M C Berman

series ordinal

1

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22 December 2017

publication date

1 December 2000

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22 December 2017

Biochimica et Biophysica Acta

number of pages

13

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based on heuristic

inferred from page(s)

published in

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22 December 2017

volume

1509

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22 December 2017

issue

1-2

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22 December 2017

page(s)

42-54

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22 December 2017

Structural organization, ion transport, and energy transduction of P-type ATPases

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Lumenal and cytoplasmic binding sites for calcium on the calcium ATPase of sarcoplasmic reticulum are different and independent

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There is only one phosphoenzyme intermediate with bound calcium on the reaction pathway of the sarcoplasmic reticulum calcium ATPase

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Ca2+ translocation across sarcoplasmic reticulum ATPase randomizes the two transported ions

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Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase

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The two calcium ions initially bound to nonphosphorylated sarcoplasmic reticulum calcium ATPase can no longer be kinetically distinguished when they dissociate from phosphorylated ATPase toward the lumen

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Calcium additional to that bound to the transport sites is required for full activation of the sarcoplasmic reticulum Ca-ATPase from skeletal muscle

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The cardiac content of sarcoplasmic reticulum in the rat determined by calcium uptake rate, calcium oxalate capacity, ryanodine binding and thapsigargin titration

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7 January 2021

Identifiers

DOI

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22 December 2017

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22 December 2017