{'fraction_non_alphanumeric': 0.02050473186119874, 'fraction_numerical': 0.0015772870662460567, 'mean_word_length': 6.129213483146067, '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}}
ADP‐Ribosylation of Highly Purified Rat Brain Mitochondria

Highly purified synaptic and nonsynaptic mitochondria were prepared from rat brain, and their ADP‐ribosyl transferase and NAD glycohydrolase activities were investigated. Data show that there is no significant difference in ADP‐ribosyl transferase activity between these two types of subcellular preparations. However, NAD glycohydrolase activity appeared to be much higher in nonsynaptic mitochondria. The specific activity of both enzymes was investigated in the presence of the inhibitor nicotinamide or its analogue 3‐aminobenzamide or other adenine nucleotides, such as ATP or ADP‐ribose. The inhibitory effect of nicotinamide or 3‐aminobenzamide on ADP‐ribosyl transferase appears rather weak compared with their effect on NAD glycohydrolase activity. However, ADP‐ribose and ATP appeared more effective in inhibiting ADP‐ribosyl transferase. Our results provide evidence for the existence of ADP‐ribosyl transferase activity in rat brain mitochondria. When NAD glycohydrolase was inhibited totally by nicotinamide, the transfer of ADP‐ribose from NAD to mitochondrial proteins still occurred. The chain length determinations show that the linkage of ADP‐ribose to mitochondrial proteins is oligomeric.