Analysis of peptide uptake inPseudomonas aeruginosa: A fluorescamine labeling procedure

Intracellular products of peptide transport were analyzed after thin layer chromatography separation by a fluorescamine labeling procedure. Dipeptides penetrated <it>Pseudomonas aeruginosa</it> via 2 transport systems, one of high affinity with <it>K</it><inf>T</inf> values from 1–2 μM, and another one of low affinity (<it>K</it><inf>T</inf> about 30 μM). A single transport system assumed tripeptide uptake with <it>K</it><inf>T</inf> varying from 10–30 μM, depending on the tripeptide used. Peptides entering the cells were rapidly hydrolyzed into their constitutive amino acids.