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. 1978 Jul 15;174(1):191-202.
doi: 10.1042/bj1740191.

The transport of alpha-aminoisobutyrate into Crithidia fasciculata

M Midgley

The transport of alpha-aminoisobutyrate into Crithidia fasciculata

M Midgley. Biochem J. .

Abstract

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.

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