Release of cytoplasmic enzymes into culture fluid
- 1 October 1974
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 84 (2) , 269-274
- https://doi.org/10.1002/jcp.1040840213
Abstract
The release of enzymatic activities from cells grown in protein‐and lipid‐free synthetic media into culture fluids was investigated. Cell strains employed were the derivatives from mouse fibroblasts, rat liver parenchymal cells, rat ascites hepatoma cells and HeLa cells. Activities of acid DNase, acid RNase and alkaline phosphatase (ALP)‐I were detected in culture fluids as early as one day after renewal of medium, whereas those of β‐glucuronidase and acid phosphatase were not found. This release of enzymes was unlikely to be caused by cell disruption during cultivation.The release of Dnase was inhibited by the addition of cycloheximide or actinbomycin D, whereas that of ALP‐I was not inhibited.Keywords
This publication has 15 references indexed in Scilit:
- Inhibition of Collagen Secretion from Bone and Cultured Fibroblasts by Microtubular Disruptive DrugsProceedings of the National Academy of Sciences, 1972
- Leakage as the source of overgrowth stimulating activity in Rous sarcoma transformed culturesExperimental Cell Research, 1971
- Proteins released from chick embryo fibroblasts in cultureExperimental Cell Research, 1970
- Increased activity of deoxyribonuclease inhibitor in rat serum after partial hepatectomyBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
- Collagen chain formation and peptidyl proline hydroxylation in monolayer tissue cultures of L-929 fibroblastsArchives of Biochemistry and Biophysics, 1969
- New Hypothesis of Insulin SecretionNature, 1968
- Hydroxylation of Proline and the Intracellular Accumulation of a Polypeptide Precursor of CollagenScience, 1966
- A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counterAnalytical Biochemistry, 1960
- Amino Acid Metabolism in Mammalian Cell CulturesScience, 1959
- Tissue fractionation studies. 4. Comparative study of the binding of acid phosphatase, β-glucuronidase and cathepsin by rat-liver particlesBiochemical Journal, 1955