Comparison of soluble and membrane-bound pyroglutamyl peptidase I activities in rat brain tissues in the presence of detergents
| Autor: | J.C. Arenas, M.A. Lopez, Francisco Alba |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Male
Octoxynol Pyroglutamyl-Peptidase I Biology Glutamyl Aminopeptidase Aminopeptidases Aminopeptidase Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology Animals Pyroglutamyl-peptidase I Solubility chemistry.chemical_classification Chromatography Aqueous solution Endocrine and Autonomic Systems Deoxycholic acid Brain Membrane Proteins Rats Inbred Strains General Medicine Microspheres Rats Enzyme Neurology Membrane protein chemistry Biochemistry Glutamyl aminopeptidase Deoxycholic Acid |
| Zdroj: | Neuropeptides. 29:103-107 |
| ISSN: | 0143-4179 |
| DOI: | 10.1016/0143-4179(95)90092-6 |
| Popis: | Pyroglutamyl peptidase I activity from soluble and membrane-bound fractions of rat brain homogenates is inhibited by the presence of sodium deoxycholate but not by triton X-100. Biobeads SM2, a polystyrene adsorbent reported to be useful in removing detergents from aqueous solutions, inhibits enzymatic activity in both fractions regardless of the presence of these detergents, probably because of partial adsorption of the enzyme by the polymeric microspheres. These effects seem to be enzyme-specific since other aminopeptidase activities are not affected by detergents or biobeads. The results suggest that soluble and membrane-bound forms of the enzyme represent the same protein in two different cell compartments. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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