The transport of alpha-aminoisobutyrate into Crithidia fasciculata.
The transport of alpha-aminoisobutyrate into Crithidia fasciculata was characterized under aerobic and anaerobic conditions. Kinetic data for alpha-aminoisobutyrate transport were consistent with the operation of a single system of broad specificity that showed no marked dependence on Na+. Under anaerobic conditions alpha-aminoisobutyrate transport was inhibited by uncouplers such as 2,4-dinitrophenol, lipophilic cations such as methyltriphenylphosphonium ion and adenosine triphosphatase inhibitors such as dicyclohexylcarbodi-imide and NaN3. A working model in which alpha-aminoisobutyrate enters this organism by an H+-symport mechanism, the electrochemical gradient of protons being maintained by an H+-translocating adenosine triphosphatase on the cytoplasmic membrane, is proposed.
D000332:Aerobiosis; D000621:Aminoisobutyric Acids / Q000378:metabolism*; D000693:Anaerobiosis; D000818:Animals; D001693:Biological Transport, Active / Q000187:drug effects; D002234:Carbodiimides / Q000494:pharmacology; D002412:Cations / Q000494:pharmacology; D003421:Crithidia / Q000378:metabolism*; D003470:Culture Media; D007700:Kinetics; D010101:Oxygen Consumption; D012977:Sodium Nitrite / Q000494:pharmacology; D014475:Uncoupling Agents / Q000494:pharmacology
D000621:Aminoisobutyric Acids; D002234:Carbodiimides; D002412:Cations; D003470:Culture Media; D014475:Uncoupling Agents; D012977:Sodium Nitrite