Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania)
| Autor: | L B Brattsten, C F Wilkinson |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Pyridines
Moths Biochemistry Mixed Function Oxygenases Spodoptera eridania chemistry.chemical_compound Microsomes Acetamides Benzene Derivatives medicine Animals Molecular Biology Oxidase test biology Metamorphosis Biological Temperature Midgut Cell Biology Hydrogen-Ion Concentration biology.organism_classification Lepidoptera Pentamethylbenzene chemistry Puromycin Larva Phenobarbital Microsome Instar Oxidoreductases 5-Aminolevulinate Synthetase Research Article medicine.drug |
| Zdroj: | Biochemical Journal. 150:97-104 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj1500097 |
| Popis: | 1. Activity of 5-aminolaevulinate synthetase was measured in the midgut and other tissues of the last larval instar of the southern armyworm (Spodoptera eridania Cramer, formerly Prodenia eridania Cramer). 2. Optimum conditions for measuring the activity were established with respect to all variables involved and considerable differences from those reported for mammalian enzyme preparations were found. 3. Maximum activity (20 nmol/h per mg of protein) occurs 18-24 h after the fifth moult and thereafter decreases to trace amounts as the larvae age and approach pupation. 4. Synthetase activity was rapidly induced by oral administration (in the diet) of pentamethylbenzene, phenobarbital, diethyl 1,4-dihydro-2,4,6-trimethylpyridine-3, 5-dicarboxylate, and 2-allyl-2-isopropylacetamide. 5. Puromycin inhibited the induction of synthetase by pentamethylbenzene. 6. Induction of 5-aminolaevulinate synthetase correlated well with the induction of microsomal N-demethylation of p-chloro-N-methylaniline, except for phenobarbital, which induced the microsomal oxidase relatively more than the synthetase. |
| Databáze: | OpenAIRE |
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