Erythrosin B (USFD&C RED 3) inhibits calcium transport and atpase activity of muscle sarcoplasmic reticulum

Stephen J. Morris; Ellen K. Silbergeld; Robin R. Brown; Duncan H. Haynes

doi:10.1016/0006-291X(82)91392-4

Erythrosin B (USFD&C RED 3) inhibits calcium transport and atpase activity of muscle sarcoplasmic reticulum

Stephen J. Morris, Ellen K. Silbergeld, Robin R. Brown, Duncan H. Haynes

Research output: Contribution to journal › Article › peer-review

27 Scopus citations

Abstract

Erythrosin B (USFD&C RED 3) inhibits the transport of calcium ions into isolated rabbit muscle sarcoplasmic reticulum vesicles with an IC₅₀ of ∼ 0.5 μM and inhibits the Ca²⁺Mg²⁺ ATPase activity with an IC₅₀ of ∼ 1 μM. The dye also binds to this tissue with an apparent K_d of ∼ 300 nM. Other iodinated and brominated fluorescein analogs and blue dextran also inhibit ATPase activity and displace bound dye, suggesting that erythrosin may bind to a site near to but not identical with the nucleotide site. The dye should prove to be a useful probe for transport and ATPase activity.

Original language	English (US)
Pages (from-to)	1306-1311
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	104
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(82)91392-4
State	Published - Feb 26 1982
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(82)91392-4

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title = "Erythrosin B (USFD&C RED 3) inhibits calcium transport and atpase activity of muscle sarcoplasmic reticulum",

abstract = "Erythrosin B (USFD&C RED 3) inhibits the transport of calcium ions into isolated rabbit muscle sarcoplasmic reticulum vesicles with an IC50 of ∼ 0.5 μM and inhibits the Ca2+Mg2+ ATPase activity with an IC50 of ∼ 1 μM. The dye also binds to this tissue with an apparent Kd of ∼ 300 nM. Other iodinated and brominated fluorescein analogs and blue dextran also inhibit ATPase activity and displace bound dye, suggesting that erythrosin may bind to a site near to but not identical with the nucleotide site. The dye should prove to be a useful probe for transport and ATPase activity.",

author = "Morris, {Stephen J.} and Silbergeld, {Ellen K.} and Brown, {Robin R.} and Haynes, {Duncan H.}",

note = "Funding Information: Drs. R. Wayne Albers and Sally M. Anderson this work was supported by NIH grant no.",

year = "1982",

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language = "English (US)",

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TY - JOUR

T1 - Erythrosin B (USFD&C RED 3) inhibits calcium transport and atpase activity of muscle sarcoplasmic reticulum

AU - Morris, Stephen J.

AU - Silbergeld, Ellen K.

AU - Brown, Robin R.

AU - Haynes, Duncan H.

N1 - Funding Information: Drs. R. Wayne Albers and Sally M. Anderson this work was supported by NIH grant no.

PY - 1982/2/26

Y1 - 1982/2/26

N2 - Erythrosin B (USFD&C RED 3) inhibits the transport of calcium ions into isolated rabbit muscle sarcoplasmic reticulum vesicles with an IC50 of ∼ 0.5 μM and inhibits the Ca2+Mg2+ ATPase activity with an IC50 of ∼ 1 μM. The dye also binds to this tissue with an apparent Kd of ∼ 300 nM. Other iodinated and brominated fluorescein analogs and blue dextran also inhibit ATPase activity and displace bound dye, suggesting that erythrosin may bind to a site near to but not identical with the nucleotide site. The dye should prove to be a useful probe for transport and ATPase activity.

AB - Erythrosin B (USFD&C RED 3) inhibits the transport of calcium ions into isolated rabbit muscle sarcoplasmic reticulum vesicles with an IC50 of ∼ 0.5 μM and inhibits the Ca2+Mg2+ ATPase activity with an IC50 of ∼ 1 μM. The dye also binds to this tissue with an apparent Kd of ∼ 300 nM. Other iodinated and brominated fluorescein analogs and blue dextran also inhibit ATPase activity and displace bound dye, suggesting that erythrosin may bind to a site near to but not identical with the nucleotide site. The dye should prove to be a useful probe for transport and ATPase activity.

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Erythrosin B (USFD&C RED 3) inhibits calcium transport and atpase activity of muscle sarcoplasmic reticulum

Abstract

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