The multiple forms of brain acetycholinesterase
✍ Scribed by G. Hüther; H. Luppa
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 581 KB
- Volume
- 63
- Category
- Article
- ISSN
- 1432-119X
No coin nor oath required. For personal study only.
✦ Synopsis
The multiple forms of acetylcholinesterase (AChE, E.C. 3.1.1.7) have been investigated with regard to their histochemical demonstrability. Their pattern is influenced by buffer treatment, fixation, and by incubation conditions causing aggregation and disaggregation as well as loss or inactivation of individual forms. The standard histochemical method for AChE preferentially demonstrates the high molecular forms. Most of the oligomer forms are washed out or inactivated. A selective demonstration of the highly aggregated forms is possible either by inhibition of the oligomers with diisopropylfluoridate (DFP) or by specifically dissolving them out. No reason could be found for the selective demonstration of the low molecular weight forms.
📜 SIMILAR VOLUMES
Four distinct N-myristoyl transferase (NMT) activity peaks, designated I, II, III, and IV, were separated from the cytosolic fraction of bovine brain by DEAE-Sepharose column chromatography. Peaks I, II, III and IV were characterised biochemically with respect to substrate specificity: with cAMP-dep