{'fraction_non_alphanumeric': 0.040892193308550186, 'fraction_numerical': 0.027881040892193308, 'mean_word_length': 4.638743455497382, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 1, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
[Creatine induction of creatine kinase synthesis in a developing monolayer culture of muscle cells].

Creatine action on the activity of creatine kinase (ATP: creatine-phosphotransferase; EC 2.7.3.2) and the content of water-soluble proteins in the developing monolayer culture of chick myoblasts are studied. Creatine at concentrations of 1.9-10- minus 3-3.8-10- minus 3 M is shown to increase reliably the creatine kinase activity by 1,1--2,9 times and to reduct considerably the content of water-soluble proteins. Lower concentrations of creatine (3.8-10- minus 5 M) also increased the creatine kinase activity but did not change the contents of water-soluble proteins. The creatine effect was maximal at the period preceding the termination of tissue cells differentiation. In the course of the combined effect of both actinomycin D (50 mcg/plate) and creatine (3.8-10- minus 3 M) the creatine kinase activity was much higher than that in the presence of actinomycin D alone which considerably reduced the enzyme activity as well as the contents of water-soluble proteins.