Adenylate cyclase activity is decreased in chick embryo fibroblasts transformed by wild type and temperature sensitive Schmidt-Ruppin Rous sarcoma virus
| Autor: | Wayne B. Anderson, Elizabeth Lovelace, Ira Pastan |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Genetics
Microbial animal structures viruses Biophysics Adenylate kinase Chick Embryo Biology Biochemistry Avian sarcoma virus Fluorides Enzyme activator Animals Magnesium Molecular Biology chemistry.chemical_classification Rous sarcoma virus Temperature Wild type Phosphorus Isotopes Cell Biology Fibroblasts biology.organism_classification Molecular biology Enzyme assay Enzyme Activation Kinetics Cell Transformation Neoplastic Enzyme Avian Sarcoma Viruses chemistry Mutation embryonic structures biology.protein Cyclase activity Adenylyl Cyclases |
| Zdroj: | Biochemical and Biophysical Research Communications. 52:1293-1299 |
| ISSN: | 0006-291X |
| Popis: | Chick embryo fibroblasts (CEF) transformed by the Schmidt-Ruppin strain of Rous sarcoma virus (RSV-SR) have decreased adenylate cyclase activity. In cells infected by a temperature-sensitive mutant of this virus (RSV-SR-T5), enzyme activity is near normal when the cells are grown at the non-permissive temperature (41°C) but decreases at the permissive temperature (36°). Adenylate cyclase activity decreases slowly over a 24 hr period to one half normal levels when CEF-RSV-SR-T5 are shifted from 41° to 36°C. The low enzyme activity in CEF-RSV-SR is not due to an alteration in the K m ATP or a change in the kinetics of Mg ++ activation, and is not observed when the enzyme is assayed in the presence of NaF. We conclude that transformation by RSV-SR reduces adenylate cyclase activity by a different mechanism than the Bryan high-titer strain of RSV. |
| Databáze: | OpenAIRE |
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