| First Author | Raisonnier A | Year | 1995 |
| Journal | Comp Biochem Physiol B Biochem Mol Biol | Volume | 111 |
| Issue | 3 | Pages | 385-98 |
| PubMed ID | 7613763 | Mgi Jnum | J:28339 |
| Mgi Id | MGI:75957 | Doi | 10.1016/0305-0491(95)00006-t |
| Citation | Raisonnier A, et al. (1995) Comparison of the cDNA and amino acid sequences of lipoprotein lipase in eight species. Comp Biochem Physiol Biochem Mol Biol 111(3):385-98 |
| abstractText | 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. |
