COMPETITION BETWEEN AMINO ACIDS FOR TRANSPORT INTO EHRLICH ASCITES CARCINOMA CELLS
- 1 November 1961
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry and Physiology
- Vol. 39 (11) , 1717-1735
- https://doi.org/10.1139/o61-190
Abstract
The cumulative entry of amino acids into Ehrlich ascites carcinoma cells is due to the presence of active transport systems, each with its own specific range of substrates. Several amino acids and amino acid analogues may have an affinity for the same transport system and thus may inhibit transport of other amino acids by acting as competitive inhibitors or competitive substrates. Loss of methionine from ascites cells takes place by a diffusion process which obeys Fick's law. Leucine accumulation by ascites cells is small and is increased on addition of certain other amino acids. The increase is not due to inhibition of leucine oxidation as increase in the rate of production of radioactive carbon dioxide from labeled leucine also occurs. Kinetic aspects of these results are discussed.Keywords
This publication has 8 references indexed in Scilit:
- Factors Controlling the Uptake and Retention of Methionine and Ethionine by Ehrlich Ascites Carcinoma CellsJournal of Biological Chemistry, 1961
- Exchange Diffusion, Transport, and Intracellular Level of Amino Acids in Ehrlich Carcinoma CellsJournal of Biological Chemistry, 1958
- CONCENTRATION WORK AND ENERGY DISSIPATION IN ACTIVE TRANSPORT OF GLYCINE INTO CARCINOMA CELLSJournal of Biological Chemistry, 1957
- BACTERIAL PERMEASESMicrobiology and Molecular Biology Reviews, 1957
- KINETIC STUDIES ON THE “INFLUX” OF GLYCINE-1-C14 INTO THE EHRLICH MOUSE ASCITES CARCINOMA CELLJournal of Biological Chemistry, 1954
- AMINO ACID CONCENTRATION BY A FREE CELL NEOPLASM. STRUCTURAL INFLUENCESJournal of Biological Chemistry, 1954
- CONCENTRATIVE UPTAKE OF AMINO ACIDS BY THE EHRLICH MOUSE ASCITES CARCINOMA CELLJournal of Biological Chemistry, 1952
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934