{'fraction_non_alphanumeric': 0.02964254577157803, 'fraction_numerical': 0.013949433304272014, 'mean_word_length': 5.1063829787234045, '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}}
The presence/absence of Bcl-2, Ca2+/calmodulin-dependent protein kinase IV, calretinin and p53 in baker's yeast and wheat germ.

After removing the nonspecific immunoreactivities from crude extracts of Saccharomyces cerevisiae and wheat germ by immunoaffinity chromatography, the presence of Ca(2+)-related proteins was tested by Western blot analysis. Immunoreactivity for Bcl-2 was absent in the yeast, whereas the immunoreactivity was evident in wheat germ and remained unchanged after incubation for 4 h with or without actinomycin D. Such incubation caused the degradation of immunoreactive-peptides of Ca2+/calmodulin-dependent protein kinase IV (CaMPK IV) in the yeast and wheat germ. Calretinin and p53 were absent in the yeast and wheat germ. The level of cyclic AMP in the yeast increased 100% after incubation for 30 min with actinomycin D. These results suggest that actinomycin D may not affect intracellular levels of these calcium-related proteins in the yeast and wheat germ, and that Bcl-2 occurs in multicellular eukaryotes. Moreover, the cellular level of CaMPK IV may vary during the onset of cell division and differentiation.