{'fraction_non_alphanumeric': 0.032879818594104306, 'fraction_numerical': 0.015873015873015872, 'mean_word_length': 4.660256410256411, '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}}
[Characteristics of microsome-bound lactate dehydrogenase from skate white muscles].

Microsomes possessing the lactate dehydrogenase (LDH) activity were isolated from white driving muscles of the skate (Raja clavata) using differential centrifugation. It was shown that the increase of the ionic strength after addition of 0.6 M KCl and alkalinization of the medium result in the solubilization of the LDH activity - by 50% and 80%, respectively. The Km values for pyruvate and NADH are 171 microM and 7.5 mM, respectively. Membrane-bound LDH, is not inhibited by pyruvate excess (up to 20 mM); the rate of the enzyme inactivation by trypsin is 3 times as low as that of the solubilized enzyme. The existence of two-membrane-bound LDH pools is postulated. The enzyme from the first pool is bound to the membrane by electrostatic whereas the second pool LDH - by hydrophobic forces.