{'fraction_non_alphanumeric': 0.02609992542878449, 'fraction_numerical': 0.013422818791946308, 'mean_word_length': 5.017937219730942, '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}}
GENETIC CONTROL OF HEPATIC 8-AMINOLEVULINATE DEHYDRATASE IN MICE1

HE enzyme 6-aminolevulinate dehydratase (5-aminolevulinate hydro-lyase E C 4.2.1.24) effects the condensation of two molecules of 8-aminolevulinate (ALA) to form porphobilinogen. It has been suggested that this enzyme may regulate the rate of porphyrin biosynthesis by allowing increased amounts of ALA to form porphyrins rather than letting it be degraded by the succinate glycine cycle (ONISAWA and LABBE 1962). In a study of the hepatic activity of this enzyme in mice with hereditary anemias (R. N. SCHIMKE and D. L. COLEMAN, unpublished results), it became apparent that several normal, nonanemic strains of mice shows reproducible inter-strain differences in hepatic activity of the enzyme. The various inbred strains tested could be classified into three groups, high, low, and intermediate with respect to their ALA dehydratase activities. Experiments demonstrating the induction of this enzyme with substrate have been reported using noninbred mice which had ALA dehydratase activities somewhat lower than the group which was found to be low in our studies (ONISAWA and LABBE 1962). This report deals with a genetic analysis of the factors involved in the control and development of this enzyme and with attempts to induce this enzyme in two inbred strains of mice.