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Ancient origin of lactalbumin from lysozyme: analysis of DNA and amino acid sequences.
Department of Biochemistry, University of California, Berkeley 94720.
Parsimony trees relating DNA sequences coding for lysozymes c and alpha-lactalbumins suggest that the gene duplication that allowed lactalbumin to evolve from lysozyme preceded the divergence of mammals and birds. Comparisons of the amino acid sequences of additional lysozymes and lactalbumins are consistent with this view. When all base positions are considered, the probability that the duplication leading to the lactalbumin gene occurred after the start of mammalian evolution is estimated to be 0.05-0.10. Elimination of the phylogenetic noise generated by fast evolution and compositional bias at third positions of codons reduced this probability to 0.002-0.03. Thus the gene duplication may have long preceded the acquisition of lactalbumin function.
PMID: 3146643 [PubMed - indexed for MEDLINE]
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Cited by 14 PubMed Central articles
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Extreme primary and secondary protein structure variability in the chimeric male-transmitted cytochrome c oxidase subunit II protein in freshwater mussels: evidence for an elevated amino acid substitution rate in the face of domain-specific purifying selection.
Chapman EG, Piontkivska H, Walker JM, Stewart DT, Curole JP, Hoeh WR.
BMC Evol Biol. 2008 May 31; 8:165. Epub 2008 May 31.
[BMC Evol Biol. 2008]
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Blackledge TA, Gillespie RG.
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[Proc Natl Acad Sci U S A. 2004]
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Koonin EV, Makarova KS, Rogozin IB, Davidovic L, Letellier MC, Pellegrini L.
Genome Biol. 2003; 4(3):R19. Epub 2003 Feb 28.
[Genome Biol. 2003]
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