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  • Title: Comparison of the cDNA and amino acid sequences of lipoprotein lipase in eight species.
    Author: Raisonnier A, Etienne J, Arnault F, Brault D, Noé L, Chuat JC, Galibert F.
    Journal: Comp Biochem Physiol B Biochem Mol Biol; 1995 Jul; 111(3):385-98. PubMed ID: 7613763.
    Abstract:
    By aligning nucleotide and amino acid sequences of lipoprotein lipase in eight species (man, pig, cow, sheep, mouse, rat, guinea-pig and chicken), we found that the main domains (catalytic, N-glycosylation and putative heparin binding sites) are well conserved. The longest identical amino acid chain was encoded by a sequence between the end of exon 2 and the beginning of exon 3, emphasizing the importance of this region which encodes the beta 5-loop of the active site, among other domains. Exon 10 is entirely untranslated in the seven mammals studied here and contains species-characteristic deletions, insertions or elements rich in A or A + T. In chicken, the beginning of exon 10 is translated. These eight previously unreported alignments could be a useful tool for further studies on LPL function.
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