Properties of phospholipase C in isolated olfactory cilia from the channel catfish (Ictalurus punctatus)
| Autor: | Taufiqul Huque, Ardithanne G. Boyle, Young S. Park, Richard C. Bruch |
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| Rok vydání: | 1987 |
| Předmět: |
Physiology
Biology Biochemistry Epithelium chemistry.chemical_compound Olfactory Mucosa medicine Animals Inositol Cilia Inositol phosphate Molecular Biology Catfishes Glycoproteins chemistry.chemical_classification Phospholipase C General Medicine biology.organism_classification Ictaluridae Molecular Weight Kinetics Microscopy Electron Enzyme Tubulin medicine.anatomical_structure chemistry Ictalurus Type C Phospholipases biology.protein Olfactory epithelium Catfish |
| Zdroj: | Comparative biochemistry and physiology. B, Comparative biochemistry. 88(3) |
| ISSN: | 0305-0491 |
| Popis: | 1. 1. Cilia were isolated from the olfactory epithelium of the channel catfish ( Ictalurus punctatus ) with improved yield. The isolated preparations were enriched in cilia as indicated by electron microscopy, tubulin immunoblotting and identification of a ciliary-specific glycoprotein. 2. 2. The isolated cilia preparations exhibited phospholipase C (EC 3.1.4.11) activity. The enzyme was maximally active at pH 6.7. 3. 3. Analysis of inositol phosphates resulting from the hydrolysis of exogenous radiolabeled phosphatidylinositol-4,5-bisphosphate in isolated cilia, indicated that inositol triphosphate was the major (90%) inositol phosphate produced. 4. 4. Three molecular forms of the enzyme, M r ≥ 100,000, 82,000 and 60,000 were resolved by gel filtration chromatography from a cytosolic fraction from the olfactory epithelium. |
| Databáze: | OpenAIRE |
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