Aberrant, canavanyl protein formation and the ability to tolerate or utilize L-canavanine
| Autor: | J. A. Bleiler, Milan A. Berge, Gerald A. Rosenthal, T. P. Rudd |
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| Rok vydání: | 1987 |
| Předmět: |
Insecta
Arginine Sphingidae Moths Butyric acid Canavanine Cellular and Molecular Neuroscience chemistry.chemical_compound Species Specificity Biosynthesis Animals Carbon Radioisotopes Molecular Biology Pharmacology biology fungi Cell Biology Metabolism Plants biology.organism_classification Lepidoptera chemistry Biochemistry Manduca sexta Larva Canavalia ensiformis Molecular Medicine |
| Zdroj: | Experientia. 43:558-561 |
| ISSN: | 1420-9071 0014-4754 |
| DOI: | 10.1007/bf02143585 |
| Popis: | L-Canavanine, 2-amino-4-(guanidinooxy)butyric acid, and L-arginine incorporation into de novo synthesized proteins was compared in six organisms. Utilizing L-[guanidinooxy14C]canavanine and L-[guanidino14C]arginine at substrate saturation, the canavanine to arginine incorporation ratio was determined in de novo synthesized proteins. Caryedes brasiliensis and Sternechus tuberculatus, canavanine utilizing insects; Canavalia ensiformis, a canavanine storing plant; and to a lesser extent Heliothis virescens, a canavanine resistant insect, failed to accumulate significant canavanyl proteins. By contrast, Manduca sexta, a canavanine-sensitive insect, and Glycine max, a canavanine free plant, readily incorporated canavanine into newly synthesized proteins. This study supports the contention that the incorporation of canavanine into proteins in place of arginine contributes significantly to canavanine's antimetabolic properties. |
| Databáze: | OpenAIRE |
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