{'fraction_non_alphanumeric': 0.027357811375089993, 'fraction_numerical': 0.0064794816414686825, 'mean_word_length': 5.405529953917051, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Effects of lincomycin on synthesis of TEM beta-lactamase by Escherichia coli.

Sub-inhibitory concentrations of lincomycin slightly inhibit growth of Escherichia coli carrying plasmid RP4 and cause a 2-fold increase in TEM-2 beta-lactamase. To analyze this effect, cultures were pulse-labeled with [3H]leucine, chased with non-radioactive leucine and immunoprecipitated with anti-beta-lactamase antiserum. The synthesis rate of beta-lactamase was two times higher in inhibited cultures than in control cultures. No significant decrease of labeled enzyme occurred during the 30 minutes chase, indicating no degradation of beta-lactamase. The rate of maturation of pre-beta-lactamase was determined by measuring the decrease in the amount of pre-beta-lactamase after a 1-minute labeling interval. There was no significant difference between the control and lincomycin-treated cultures, indicating that posttranslational translocation is not involved in the stimulation. Both plasmid encoded and chromosomally encoded TEM-1 beta-lactamase increased in the presence of lincomycin. The effects of other protein synthesis inhibitors on the synthesis of TEM-1 beta-lactamase were examined. The stimulation of beta-lactamase synthesis by lincomycin appears to be specific for macrolide and related antibiotics and is not a general phenomenon resulting from partial inhibition of protein synthesis.