Phosphorylation of component a of the human erythrocyte membrane in myotonic muscular dystrophy

Allen D. Roses; Stanley H. Appel

doi:10.1007/BF01870627

Phosphorylation of component a of the human erythrocyte membrane in myotonic muscular dystrophy

Allen D. Roses, Stanley H. Appel

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

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Abstract

Endogenous membrane protein kinase activity in fresh erythrocyte ghosts is altered in myotonic muscular dystrophy. Phosphorylation of erythrocyte Component a, which migrates with an apparent molecular weight of 90,000 to 100,000, is significantly reduced compared to age- and sex-matched controls. The difference in endogenous membrane protein kinase activity in fresh RBC membranes lends confirmation to the suggestion that myotonic dystrophy is a disease of widespread membrane alterations.

Original language	English (US)
Pages (from-to)	51-58
Number of pages	8
Journal	The Journal of Membrane Biology
Volume	20
Issue number	1
DOIs	https://doi.org/10.1007/BF01870627
State	Published - Dec 1 1975

ASJC Scopus subject areas

Biophysics
Physiology
Cell Biology

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10.1007/BF01870627

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abstract = "Endogenous membrane protein kinase activity in fresh erythrocyte ghosts is altered in myotonic muscular dystrophy. Phosphorylation of erythrocyte Component a, which migrates with an apparent molecular weight of 90,000 to 100,000, is significantly reduced compared to age- and sex-matched controls. The difference in endogenous membrane protein kinase activity in fresh RBC membranes lends confirmation to the suggestion that myotonic dystrophy is a disease of widespread membrane alterations.",

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N2 - Endogenous membrane protein kinase activity in fresh erythrocyte ghosts is altered in myotonic muscular dystrophy. Phosphorylation of erythrocyte Component a, which migrates with an apparent molecular weight of 90,000 to 100,000, is significantly reduced compared to age- and sex-matched controls. The difference in endogenous membrane protein kinase activity in fresh RBC membranes lends confirmation to the suggestion that myotonic dystrophy is a disease of widespread membrane alterations.

AB - Endogenous membrane protein kinase activity in fresh erythrocyte ghosts is altered in myotonic muscular dystrophy. Phosphorylation of erythrocyte Component a, which migrates with an apparent molecular weight of 90,000 to 100,000, is significantly reduced compared to age- and sex-matched controls. The difference in endogenous membrane protein kinase activity in fresh RBC membranes lends confirmation to the suggestion that myotonic dystrophy is a disease of widespread membrane alterations.

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Phosphorylation of component a of the human erythrocyte membrane in myotonic muscular dystrophy

Abstract

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