{'fraction_non_alphanumeric': 0.02956081081081081, 'fraction_numerical': 0.03462837837837838, 'mean_word_length': 4.925, '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}}
MOLECULAR ANALYSIS OF THE STEROIDOGENIC 11β-HYDROXYLASE ENZYME

We have isolated bovine cDNA clones corresponding to a full length mRNA encoding cytochrome P-450 (11βOH), using a short previously described clone (John et al, J Biol Chem 260:5760) and a size-fractionated library enriched for full length 11βOH cDNA. Sequence analysis shows an open reading frame of 1500 nucleotides which contains the highly conserved heme-binding region and shows 40% homology to cytochrome P-450 (SCC) at the amino acid level. The open reading frame contains sequences corresponding to several tryptic peptides of the porcine enzyme (J, Shively, pers comm). Several human cDNA clones have been isolated, the longest of which is 3700 base pairs (bp). Hybridization analysis with human genomic DNA suggests that the gene is present in a single copy and is about 18 kbp. Analysis of genomic DNA from four patients with 11β-hydroxylase deficiency shows no gross deletions or rearrangements within the structural gene. Hybridization to a panel of somatic cell hybrid cell lines indicates that the gene is on a chromosome distinct from the other steroidogenic P-450 genes (which are on Chr 6, 10, and 15).