Isolation of an abnormally phosphorylated erythrocyte membrane band 3 glycoprotein from patients with myotonic muscular dystrophy
- 1 March 1979
- journal article
- research article
- Published by Springer Nature in The Journal of Membrane Biology
- Vol. 45 (1-2), 147-166
- https://doi.org/10.1007/bf01869299
Abstract
A fraction of erythrocyte Band 3 (M r , 93,000) glycoprotein that demonstrates decreased autophosphorylation in membranes from myotonic muscular dystrophy patients is demonstrated. Sequential affinity chromatography of Triton X-100 solubilized erythrocyte membrane proteins separated three specifically retained glycoprotein fractions on a Ricin Communis I-Sepharose 4B column. One fraction contains a portion of the major sialoglycoprotein (apparentM r , 78,000) and is specifically eluted from the column by 10mm NaCl and 100mm d-galactose (10/100). The two other glycoprotein fractions are eluted by 100mm NaCl, 10mm d-galactose (100/10) and 100mm NaCl, 100mm d-galactose (100/100). The composition of both fractions contains greater than 95% Band 3 (apparentM r , 93,000) glycoprotein. The quantities of glycoprotein in each fraction obtained from erythrocytes of myotonic dystrophy patients did not differ from the quantities obtained from control erythrocytes. Following endogenous protein kinase incubations of ghosts with [γ-32P]ATP, the specific [32P] phosphorylation of the 10/100 and 100/10 fractions are identical. The 100/100 fraction, which makes up approximately 3% of the total erythrocyte membrane protein, demonstrates a different pattern for myotonic dystrophy patients; specific phosphorylation was reduced by 50% relative to activity in control experiments. These findings are consistent with previous experiments that demonstrated decreased autophosphorylation of the glycoprotein portion of Band 3 (Roses & Appel, 1975,J. Membrane Biol. 20: 51) and are consistent with the autosomal dominant mode of inheritance in this disease.This publication has 40 references indexed in Scilit:
- Increased phosphorylated components of erythrocyte membrane spectrin band II with reference to Duchenne muscular dystrophyJournal of the Neurological Sciences, 1976
- Elucidation of lectin receptors by quantitative inhibition of lectin binding to human erythrocytes and lymphocytesBiochemistry, 1976
- Erythrocyte spectrin peak II phosphorylation in Duchenne muscular dystrophyJournal of the Neurological Sciences, 1976
- Proteolytic dissection of band 3, the predominant transmembrane polypeptide of the human erythrocyte membraneBiochemistry, 1976
- Substrate heterogeneity of component a of the human erythrocyte membraneJournal of Supramolecular Structure, 1976
- Phosphorylation of component a of the human erythrocyte membrane in myotonic muscular dystrophyThe Journal of Membrane Biology, 1975
- Solubilization of membranes by detergentsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1975
- Characterization of two plant lectins from Ricinus communis and their quantitative interaction with a murine lymphomaBiochemistry, 1974
- Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergentsJournal of Supramolecular Structure, 1973
- Disposition of the major proteins in the isolated erythrocyte membrane. Proteolytic dissectionBiochemistry, 1971