Abstract
1. Amebae contain DPN at levels of from 1 to 4 x 10–13 moles per cell. 2. Following enucleation, nucleate and enucleate halves continue to have equal DPN contents over the six day period studied. Similarly, starving whole amebae maintain their DPN level over this period. 3. No reduced DPN could be detected in these aerobic animals. This remained true for whole amebae and for nucleate and enucleate halves over 5 days of starvation. 4. A method is described for the preparation and rapid separation of nucleate and enucleate ameba halves, based on a response of amebae to light.
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Selected References
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- ALLFREY V., STERN H., MIRSKY A. E., SAETREN H. The isolation of cell nuclei in non-aqueous media. J Gen Physiol. 1952 Jan;35(3):529–554. doi: 10.1085/jgp.35.3.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BALTUS E. Observations sur le rôle biochimique du nucléole. Biochim Biophys Acta. 1954 Oct;15(2):263–267. doi: 10.1016/0006-3002(54)90068-2. [DOI] [PubMed] [Google Scholar]
- BRACHET J. Oxygen uptake of nucleated and non-nucleated halves of Amoeba proteus. Nature. 1951 Aug 4;168(4266):205–205. doi: 10.1038/168205a0. [DOI] [PubMed] [Google Scholar]
- COLOWICK S. P., KAPLAN N. O., CIOTTI M. M. The reaction of pyridine nucleotide with cyanide and its analytical use. J Biol Chem. 1951 Aug;191(2):447–459. [PubMed] [Google Scholar]
- GREENGARD P., BRINK F., Jr, COLOWICK S. P. Some relationships between action potential, oxygen consumption and coenzyme content in degenerating peripheral axons. J Cell Physiol. 1954 Dec;44(3):395–420. doi: 10.1002/jcp.1030440304. [DOI] [PubMed] [Google Scholar]
- HOGEBOOM G. H., SCHNEIDER W. C. Cytochemical studies. VI. The synthesis of diphosphopyridine nucleotide by liver cell nuclei. J Biol Chem. 1952 May;197(2):611–620. [PubMed] [Google Scholar]
- LOWRY O. H., ROBERTS N. R., WU M. L., HIXON W. S., CRAWFORD E. J. The quantitative histochemistry of brain. II. Enzyme measurements. J Biol Chem. 1954 Mar;207(1):19–37. [PubMed] [Google Scholar]
- LePAGE G. A., SCHNEIDER W. C. Centrifugal fractionation of glycolytic enzymes in tissue homogenates. J Biol Chem. 1948 Dec;176(3):1021–1027. [PubMed] [Google Scholar]
- MAZIA D., HIRSHFIELD H. I. The nucleus-dependence of P32 uptake by the cell. Science. 1950 Sep 15;112(2907):297–299. doi: 10.1126/science.112.2907.297. [DOI] [PubMed] [Google Scholar]
- OCHOA S., STERN J. R. Carbohydrate metabolism. Annu Rev Biochem. 1952;21:547–602. doi: 10.1146/annurev.bi.21.070152.002555. [DOI] [PubMed] [Google Scholar]
- STERN H., MIRSKY A. E. The isolation of wheat germ nuclei and some aspects of their glycolytic metabolism. J Gen Physiol. 1952 Nov;36(2):181–200. doi: 10.1085/jgp.36.2.181. [DOI] [PMC free article] [PubMed] [Google Scholar]