{'fraction_non_alphanumeric': 0.011797752808988765, 'fraction_numerical': 0.017977528089887642, 'mean_word_length': 4.726688102893891, '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}}
Hemoglobin 3 chains in apes. Primary structures and the presumptive nature of back mutation in a normally silent gene.

Abstract The amino acid sequence of an unusual adult hemoglobin chain, termed 3α, is delineated for 107 of 141 residues from gorilla. The sequence of the remainder of positions from gorilla as well as those in a similar 3α chain from chimpanzee are inferred from peptide composition and homology with the sequence of the major α chains. The eight to nine amino acid differences between 3α and the major α chains are scattered throughout the chain and similar for both gorilla and chimpanzee proteins. The extent of the differences suggests that the genesis of the 3α gene much antedated speciation among the great apes and that man, in whom 3α chains have not yet been detected, may also possess the 3α locus. Trace hemoglobins containing 3α chains were found, among 14 gorillas in only a father and son; a comparable hemoglobin was found only once among 37 chimpanzees. Electrophoretic and immunological features suggest that 3α gene products are indeed absent in most animals and not merely rendered undetectable by the mass of hemoglobin A. A clue to the inactivity of the 3α gene in most animals and its appearance in a few is the occurrence of serine/asparagine or aspartic acid heterogeneity at position 131, 133, or 138 of the 3α chain from one gorilla. Such heterogeneity suggests that two allele products are produced. Genetic and other features make it unlikely that this biallelic expression is the result of a reversion mutation in each of two 3α alleles and support the notion that 3α products are normally absent because of a nearly ubiquitous nonsense mutation which has been suppressed in a few animals by mutation at some non-hemoglobin locus.