{'fraction_non_alphanumeric': 0.0314192849404117, 'fraction_numerical': 0.010834236186348862, 'mean_word_length': 5.553191489361702, '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}}
Identification and partial purification of phosphatidylcholine phospholipase C from the cryptobiotic cysts of the fairy shrimp, Streptocephalus dichotomus.

The occurrence of phosphatidyl choline specific phospholipase C (PC-PLC)(EC 3.1.4.3) which liberates diacylglycerol (DAG), an important second messenger molecule, has been reported for the first time from the cryptobiotic cysts of the fairy shrimp, Streptocephalus dichotomus. Since the cysts undergo a revival of metabolism and resumption of development upon hydration, the possible role of the enzyme, in these processes was investigated. The results revealed enzyme's presence and an increase in its activity with the advancement of cyst development. Further partial purification of the enzyme using a lipoprotein linked- Sepharose CL-4B column (an affinity chromatographic principle) was attempted. The purification of 19.3 fold with a yield of 80% was attained.