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Acetylation of erythrocytic membrane peptides by aspirin
Author(s) -
Green F.A.,
Jung C.Y.
Publication year - 1981
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1981.21181127484.x
Subject(s) - membrane , acetylation , aspirin , sodium dodecyl sulfate , peptide , chemistry , gel electrophoresis , polyacrylamide gel electrophoresis , biochemistry , size exclusion chromatography , sodium , chromatography , enzyme , gene , organic chemistry
Acetylation of erythrocytic membranes by aspirin has not been reported. When erythrocytes or erythrocytic membranes are incubated with [acetyl‐ 14 C]aspirin, there is good evidence of very tight binding to membrane peptides in concentrations known to occur in vivo , 20 to 200 µM. No such evidence is observed with [carboxy‐ 14 C] aspirin. This indicates acetylation of membrane peptides. Although pronounced selectivity is not observed among the different peptides by gel filtration on Bio‐Gel A‐5M and sodium dodecyl sulfate polyacrylamide gel electrophoresis, there is overall saturation with a half‐maximum at about 10 mM. The clinical significance of acetylation of membrane peptides of erythrocytes is unclear.