Abstract
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 μM. The binding was inhibited by p‐chloromercuribenzoate and the inhibition was reversed by dithiothreitol.