Cobra Venom Acetylcholinesterase: Nature of Charge Isoforms
- 3 March 2005
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 127 (3) , 507-512
- https://doi.org/10.1111/j.1432-1033.1982.tb06900.x
Abstract
Charge isoforms of cobra (N. n. oxiana) venom acetylcholinesterase, separated by isoelectric focusing, differ only by the number of free carboxyl groups of glutamic and/or aspartic acid side-chains in the enzyme molecule. The isoforms appear to be produced by a post-translational deamidation of accessible glutamine and/or asparagine residues. The isoforms have identical catalytic specificities towards characteristic acetylcholinesterase substrates.This publication has 31 references indexed in Scilit:
- Affinitätschromatographische reinigung und eigenschaften der acetylcholinesterase aus kobragift (naja naja atra)Journal of Chromatography A, 1979
- Charge-state and charge-continuum models in electrophoresis and isoelectric focusing of genetic variantsJournal of Chromatography A, 1979
- Cobra Venom AcetylcholinesteraseEuropean Journal of Biochemistry, 1979
- Improved procedure for peptide characterization using thin-layer chromatography and a fluorescamine indicatorJournal of Chromatography A, 1977
- Isoelectric points and molecular weights of proteinsJournal of Chromatography A, 1976
- Multiple molecular forms of snake venom phosphodiesterase from Vipera palastinaeToxicon, 1976
- Rates of nonenzymic deamidation of glutaminyl and asparaginyl residues in pentapeptidesJournal of the American Chemical Society, 1973
- On the Heterogeneity of Beef Heart Cytochrome c. III. A Kinetic Study of the Non-enzymic Deamidation of the Main Subfractions (Cy I - Cy III).Acta Chemica Scandinavica, 1966
- Hydrolysis of Carboxylic Acid Esters of Thiocholine and its Analogues. 2. Alkaline Hydrolysis.Acta Chemica Scandinavica, 1958
- Herstellung von α‐Aminosäureestern durch Alkoholyse der MethylesterHelvetica Chimica Acta, 1953