PMID: 697752Jul 15, 1978Paper

The transport of alpha-aminoisobutyrate into Crithidia fasciculata

The Biochemical Journal
M Midgley

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.

Citations

Jan 1, 1985·Zeitschrift Für Parasitenkunde·M A MillgramJ Shlomai
May 27, 1980·Biochimica Et Biophysica Acta·I C West
Apr 1, 1991·Experimental Parasitology·J A Thissen, C C Wang
Mar 1, 1980·Microbiological Reviews·R B McGhee, W B Cosgrove

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