{'fraction_non_alphanumeric': 0.026483050847457626, 'fraction_numerical': 0.014830508474576272, 'mean_word_length': 5.654929577464789, '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}}
Isolation and Characterization of a Type 1 Ribosome-Inactivating Protein from Fruiting Bodies of the Edible Mushroom (Volvariella volvacea).

A novel single-chained ribosome-inactivating protein (RIP) with a molecular weight of approximately 29 000 was purified from fruiting bodies of the edible mushroom Volvariellavolvacea with a procedure involving ammonium sulfate precipitation, ion-exchange chromatography on DEAE-cellulose, and gel filtration on Superdex 75. The mushroom RIP, designated volvarin, exhibited a potent inhibitory action on protein synthesis in the rabbit reticulocyte lysate system with an IC(50) value of 0.5 nM. Like most plant RIPs, volvarin acted as an N-glycosidase that depurinated rRNA from rabbit reticulocyte lysate, releasing a characteristic RNA fragment after treatment with aniline. It also exerted a deoxyribonuclease activity on supercoiled SV-40 DNA and demonstrated a strong abortifacient effect in mice.