Add time:08/01/2019         Source:sciencedirect.com

1.1. The properties of a sarcosine uptake system in nitrogen-starved cells of Saccharomyces chevalieri are described. The intracellular radioactivity accumulated corresponds to free sarcosine as indicated by radioautography.2.2. Internally accumulated [14C]sacrosine does not outflow when cells are resuspended in fresh buffer, but slowly exchanges with externaly added [12C]sarcosine, l-[12C]proline and d-[12C]proline.3.3. Sarcosine uptake is temperature dependent and it is strongly inhibited by 20 mM azide and 1 mM 2,4-dinitrophenol.4.4. Initial velocity of sarcosine uptake depends on external sarcosine concentration. The system shows a Michaelis-Menten substrate dependence with an apparent Km of 3.1·10−5 M. l-Proline, d-proline, dl-azetidin carboxylic acid and l-thiazolidin carboxylic acid were found to competitively inhibit the sarcosine uptake and their Ki were calculated. Among a number of amino acids only l-alanine and glycine effectively inhibit the sarcosine uptake.5.5. These experiments strongly suggest that the accumulation of l-proline and sarcosine in yeast cells are mediated by the same uptake system. Moreover, kinetics results agree with our proposition that the uptake of all imino acids in yeast is mediated by the same transport system.

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