{'fraction_non_alphanumeric': 0.02944507361268403, 'fraction_numerical': 0.007927519818799546, 'mean_word_length': 5.2695035460992905, '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}}
Deamidation in vivo of an asparagine residue of rabbit muscle aldolase.

Microheterogeneity of rabbit muscle aldolase is caused by deamidation in vivo of an asparagine residue near the C-terminus of each subunit. Isotopic labeling of a peptide containing the asparagine residue at various time intervals before isolation of aldolase permits estimation of the half-time for the deamidation as about 8 days, which is about the time estimated for the half-life of the enzyme in vivo. It is concluded that the aldolase as genetically determined is a tetramer, designated alpha(4), that undergoes random deamidation to form alpha(3)beta, alpha(2)beta(2), and alphabeta(3) species as intermediates in the formation of beta(4), the species in which all of the specific asparagine has been deamidated. Isoelectric focusing data indicate that the subunits do not exchange appreciably in vivo.