INDUCTION KINETICS OF L-ARABINOSE OPERON OF ESCHERICHIA-COLI
INDUCTION KINETICS OF L-ARABINOSE OPERON OF ESCHERICHIA-COLI
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DOI：
10.1128/jb.115.1.9-14.1973
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发表时间：
1973-01-01
影响因子：
3.2
通讯作者：
ELLIS, D
中科院分区：
文献类型：
--
作者：
SCHLEIF, R;HESS, W;ELLIS, D
After addition ofl-arabinose to growingEscherichia coli, thel-ribulokinase (EC 2.7.1.16) andl-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 β-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.
