Abstract
The trichloroacetic acid (TCA)-insoluble fraction of water column bacteria labeled with [3H]leucine contained an ethanol-soluble fraction accounting for up to 44% of the label. A component of the ethanol-soluble fraction is [3H]leucine. Labeled-protein purification requires an ethanol wash step. Cold TCA can replace hot TCA for precipitation of labeled proteins.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Chin-Leo G., Kirchman D. L. Estimating bacterial production in marine waters from the simultaneous incorporation of thymidine and leucine. Appl Environ Microbiol. 1988 Aug;54(8):1934–1939. doi: 10.1128/aem.54.8.1934-1939.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hurrell R. F., Carpenter K. J. Mechanisms of heat damage in proteins. 8. The role of sucrose in the susceptibility of protein foods to heat damage. Br J Nutr. 1977 Sep;38(2):285–297. doi: 10.1079/bjn19770089. [DOI] [PubMed] [Google Scholar]
- Kirchman D., K'nees E., Hodson R. Leucine incorporation and its potential as a measure of protein synthesis by bacteria in natural aquatic systems. Appl Environ Microbiol. 1985 Mar;49(3):599–607. doi: 10.1128/aem.49.3.599-607.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robarts R. D., Wicks R. J., Sephton L. M. Spatial and Temporal Variations in Bacterial Macromolecule Labeling with [methyl-H]Thymidine in a Hypertrophic Lake. Appl Environ Microbiol. 1986 Dec;52(6):1368–1373. doi: 10.1128/aem.52.6.1368-1373.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]