An Amphiphile-Dependent Form of Human Brain Caudate Nucleus Acetylcholinesterase: Purification and Properties
| Autor: | Urs Brodbeck, K. Sorensen, R. Gentinetta |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Octoxynol
Protein subunit Immunoelectrophoresis Biochemistry Polyethylene Glycols Cellular and Molecular Neuroscience chemistry.chemical_compound Affinity chromatography Tetramer Amphiphile Centrifugation Density Gradient medicine Humans Differential centrifugation chemistry.chemical_classification medicine.diagnostic_test Acetylcholinesterase Isoenzymes Molecular Weight Kinetics Enzyme chemistry Electrophoresis Polyacrylamide Gel Caudate Nucleus Isoelectric Focusing |
| Zdroj: | Journal of Neurochemistry. 39:1050-1060 |
| ISSN: | 1471-4159 0022-3042 |
| DOI: | 10.1111/j.1471-4159.1982.tb11496.x |
| Popis: | Different forms of acetylcholinesterase (AChE), EC 3.1.1.7, were demonstrated in human brain caudate nucleus. One form was solubilized at high ionic strength, the other with Triton X-100. The detergent-extractable form was purified to homogeneity by affinity chromatography. This form of AChE is amphiphile-dependent; i.e., it was active only in the presence of amphiphiles (detergents or lipids). Further, the enzyme was shown to bind detergents and to interact hydrophobically with Phenyl-Sepharose. In the presence of detergents the enzyme is a tetramer (subunit molecular weight, 78,000) which aggregates on the removal of detergents. Human brain AChE showed a reaction of identity with human erythrocyte AChE in crossed-line immunoelectrophoresis. The high-salt-soluble brain enzyme did not cross-react with the erythrocyte enzyme. The two classes of AChE seem not to be related, as they show no common antigenic determinant. |
| Databáze: | OpenAIRE |
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