| Title : Purification by affinity chromatography of the molecular forms of acetylcholinesterase present in fresh electric-organ tissue of electric eel - Dudai_1972_Proc.Natl.Acad.Sci.U.S.A_69_2400 |
| Author(s) : Dudai Y , Silman I , Shinitzky M , Blumberg S |
| Ref : Proceedings of the National Academy of Sciences of the United States of America , 69 :2400 , 1972 |
|
Abstract :
An acetylcholinesterase inhibitor-Sepharose conjugate was prepared by coupling a derivative of the powerful acetylcholinesterase inhibitor, N-methylacridinium, to CNBr-activated Sepharose. Use of this conjugate permitted direct purification, by affinity chromatography, of the two molecular forms of acetylcholinesterase, 14 and 18 S, present in fresh electric organ tissue. The purified 14S and 18S acetylcholinesterases retained the capacity to aggregate at low ionic strength displayed by crude extracts of the enzyme. The major polypeptide components of the 14S and 18S enzymes, as revealed by acrylamide gel electrophoresis, closely resemble those observed in the 11S form of acetylcholinesterase, previously purified after tryptic digestion of electric-organ tissue. |
| PubMedSearch : Dudai_1972_Proc.Natl.Acad.Sci.U.S.A_69_2400 |
| PubMedID: 4506759 |
Dudai Y, Silman I, Shinitzky M, Blumberg S (1972)
Purification by affinity chromatography of the molecular forms of acetylcholinesterase present in fresh electric-organ tissue of electric eel
Proceedings of the National Academy of Sciences of the United States of America
69 :2400
Dudai Y, Silman I, Shinitzky M, Blumberg S (1972)
Proceedings of the National Academy of Sciences of the United States of America
69 :2400