Temperature dependence of amino acid transport in ehrlich ascites cells: with results which bear on the A–L distinction
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 203, Issue: 1, Page: 150-166
1970
- 31Citations
- 1Captures
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Metrics Details
- Citations31
- Citation Indexes31
- CrossRef31
- 31
- Captures1
- Readers1
Article Description
We have examined the temperature dependence of maximal flux, JM, the half-saturation value, Km, and of the linear components, k, of the initial transport flux for l -methionine, l -tryptopah, glycine, l -alanine, α-aminoisobutyric acid and l -phenylalanine in Ehrlich ascites cells. For l -alanine, α-aminoisobutyric acid and l -phenylalanine we examined the initial flux in transport and in exchange for cells in Na + -containing and in Na + -free media. The maximal flux in transport falls with decrease in temperature, the activation energies falling in the range 11–20 kcal/mole. The Km decreased with decrease in temperature for l -phenylalanine and l -tryptophan with apparent activation energies of 20 and 15 kcal/mole respectively, For l -methionine, glycine and l -alanine the Km showed no dependence on temperature whereas for α-aminoisobutyric acid in increased as the temperature fell. For all amino acids, the Km appeared to be more variable a parameter of the initial flux than was the maximal flux. The results for the linear component of the uptake, k, also were highly variable, but k did decrease with a fall in temperature with activation energies falling in the range 5.8–17.7 kcal/mole.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0005273670900453; http://dx.doi.org/10.1016/0005-2736(70)90045-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0014952637&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/5445672; https://linkinghub.elsevier.com/retrieve/pii/0005273670900453; http://dx.doi.org/10.1016/0005-2736%2870%2990045-3; https://dx.doi.org/10.1016/0005-2736%2870%2990045-3
Elsevier BV
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