Conference paper

Comparative Studies on the Molecular Properties of Purified Acetylcholinesterase from Human Erythrocytes and from the Electric Organ of Electrophorus electricus

Urs Brodbeck ; Medizinisch-chemisches Institut der Universitat, Buhlstr . 28, CH- 3000 Bern 9, Switzerland
Peter Ott ; Medizinisch-chemisches Institut der Universitat, Buhlstr . 28, CH- 3000 Bern 9, Switzerland
Therese Wiedmer ; Medizinisch-chemisches Institut der Universitat, Buhlstr . 28, CH- 3000 Bern 9, Switzerland

Abstract

Acetylcholinesterases from human erythrocytes and from the
electric organ of Electrophorus electricus were purified by affinity
chromatography to high degrees of purity. The molecular parameters
of both enzymes were compared following density gradient
centrifugation, gel filtration, i.soelectric focusing and polyacrylamide
gel electrophoresis. Sucrose density gradient centrifugation revealed that the human enzyme exists in a more complex state of aggregation than the eel enzyme. Upon isoelectric focusing both enzymes could be
resolved into multiple molecular forms; the eel enzyme however
focused at a lower pH than the red cell enzyme.
The Stokes radii of the human enzyme forms range between
6.8 and 12.9 nm; the ones for the eel enzyme forms are between
6.4 and 15.0 nm. SDS ~polyacrylamide gel electrophoresis gave one
subunit only for both enzymes with apparent molecular weights
of 80 000 and 93 000 for the human and the eel enzyme respectively.

Keywords

Hrčak ID:

196585

URI

https://hrcak.srce.hr/196585

Publication date:

3.12.1975.

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