{'fraction_non_alphanumeric': 0.02895752895752896, 'fraction_numerical': 0.009652509652509652, 'mean_word_length': 5.136094674556213, '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}}
Immunological cross-reactivities between two yeast cytochromes c and the immunological reactivities of the peptide fragments of Saccharomyces oviformis M2 cytochrome c.

Cytochromes c from two strains of yeast, Saccharomyces oviformis M2 (M2-cyt. c) and Candida krusei, in their cross-reactivities against their antibodies, were investigated by various methods. The results indicated that cytochromes c from these two yeasts cross-reacted each other with their antibodies, but that horse heart cytochrome c did not cross-react. It was also suggested that the passive cutaneous anaphylaxis inhibition test is preferable to the usual in vitro methods in detecting slight difference in the cross-reactivities between closely related antigens. Another experiments using peptide fragments obtained by enzymatic or chemical cleavage of M2-cyt. c showed that P-4 and P-7 were found to fix complements, and P-3, P-4, P-5 and P-6 eliminated the inhibitory effect of the antibody against the enzymatic reaction of cytochrome c-cytochrome oxidase.