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. 1973 Jul;115(1):9-14.
doi: 10.1128/jb.115.1.9-14.1973.

Induction kinetics of the L-arabinose operon of Escherichia coli

R Schleif, W Hess, S Finkelstein, D Ellis

Induction kinetics of the L-arabinose operon of Escherichia coli

R Schleif et al. J Bacteriol. 1973 Jul.

Abstract

After addition of l-arabinose to growing Escherichia coli, the l-ribulokinase (EC 2.7.1.16) and l-arabinose isomerase (EC 5.3.1.4) first appear at about 0.7 and 1.4 min, respectively. These times are consistent with the distances of the genes from the ribonucleic acid polymerase initiation site in the operon. The kinetics of appearance of these enzymes as well as those of beta-galactosidase (EC 3.2.1.23) in the same strain are consistent with a peptide elongation rate of no less than 14 amino acids per second. A measurement of the average peptide elongation rate made by measuring the kinetics of radioactive amino acid appearance in completed polypeptides yielded a rate of about 12 amino acids per s. Convenient assays of the arabinose isomerase and ribulokinase are also given.

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References

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