N-(Phosphonacetyl)-L-aspartate-resistant hamster cells overaccumulate a single mRNA coding for the multifunctional protein that catalyzes the first steps of UMP synthesis.
Open Access
- 1 February 1979
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 254 (3) , 974-980
- https://doi.org/10.1016/s0021-9258(17)37899-7
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- An Efficient mRNA‐Dependent Translation System from Reticulocyte LysatesEuropean Journal of Biochemistry, 1976
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Elevated dihydrofolate reductase messenger RNA levels in methotrexate-resistant BHK cellsCell, 1976
- Quantitative Film Detection of 3H and 14C in Polyacrylamide Gels by FluorographyEuropean Journal of Biochemistry, 1975
- Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undegraded polysomes and messenger ribonucleic acidBiochemistry, 1974
- Dissociation by elastase digestion of enzyme complex catalyzing the initial steps of pyrimidine biosynthesis in rat liverBiochemical and Biophysical Research Communications, 1973
- Uridylic acid synthesis in Ehrlich ascites carcinoma. Properties, subcellular distribution, and nature of enzyme complexes of the six biosynthetic enzymesBiochemistry, 1973
- The transformation of BHK 21 hamster cells by simian virus 40International Journal of Cancer, 1972
- Copurification of carbamoyl phosphate synthetase and aspartate transcarbamoylase from mouse spleenBiochemical and Biophysical Research Communications, 1971