Izlaganje sa skupa

Regulatory Properties of Membrane Bound Acetylcholinesterase from Red Cell Ghosts

Helmut Kuhnen ; Fraunhofer-Gesellschaft, Institut fur Aerobiologie, D 5949 Grafschaft/Schmallenberg, B. R. Deutschland

Sažetak

Activating and inhibiting properties of quaternary pyridinium
compounds on acetylcholinesterase (AChE), bound to bovine red
cell membranes, were investigated. The action of these compounds
is mainly due to their quaternary structure, while the effect of the
substituents on the pyridinium moeity is less important. The effect
of the compounds on the rate of hydrolysis of acetyl-~-metylchoLine
(MeCh) is different from the effect on acetylcholine (ACh) hydrolys1s.
The effect of toxogonin on the structure-bound enzyme is
different from the effect on the water-soluble enzyme, the latter
not being activated by toxogonin.
V m values were determined by the method of Hofstee. Hill
plots yielded several straight lines. It Js postulated that AChE
exists in several states of cooperativity (negative, non- and positive
cooperativity). The different states are assumed to correspond to
different allosteric conformations of the protein. The reactions
of structure-bound and water-soluble enzyme are different. In
contrast to the bound form, the soluble form could not be activated.

Ključne riječi

Hrčak ID:

196619

URI

https://hrcak.srce.hr/196619

Datum izdavanja:

3.12.1975.

Posjeta: 608 *