{'fraction_non_alphanumeric': 0.029865125240847785, 'fraction_numerical': 0.023121387283236993, 'mean_word_length': 4.6775956284153, '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}}
[Determination of isoelectric points of oligomeric forms of mitochondrial creatine kinase].

Using isoelectrofocusing in three pH gradients differing in the initial pH value of the ampholyte gel mixture and in gradient pH range, the isoelectric points for the dimeric and octameric forms of mitochondrial creatine kinase from bovine heart and pigeon breast muscle were determined. The isoelectric points for the dimer and octamer are equal to 9.67 +/- 0.01 and 8.93 +/- 0.05 for the heart enzyme and to 9.56 +/- 0.08 and 8.91 +/- 0.23 for the skeletal muscle enzyme. The correctness of identification of the oligomeric forms of mitochondrial creatine kinase was confirmed by ultracentrifugation in a sucrose density linear gradient. Since creatine kinase is known to bind to mitochondrial membrane cardiolipin by electrostatic forces, it can be assumed that both oligomeric forms of the enzymes can bind to the membranes. However, the properties of the creatine kinase dimer suggest its greater ability to bind to mitochondrial membranes.