Purification and characterization of alanine carrier isolated from H-proteins of Bacillus subtilis.
Alanine transport carrier was isolated and purified from H-proteins of Bacillus subtilis. The purified carrier preparation was homogeneous in migration on polyacrylamide gels containing urea or sodium dodecyl sulfate. Electrophoresis on polyacrylamide gels containing dodecyl sulfate showed a single band of molecular weight of about 7500. 1 mol alanine was bound/mol carrier protein with a dissociation constant of 0.2 micron. The binding was inhibited by p-chloromercuribenzoate and the inhibition was reversed by dithiothreitol.
D000409:Alanine / Q000378:metabolism*; D001412:Bacillus subtilis / Q000187:drug effects / Q000378:metabolism*; D001692:Biological Transport / Q000187:drug effects; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight
D002352:Carrier Proteins; D002729:Chloromercuribenzoates; D000409:Alanine; D004229:Dithiothreitol