Raisonnier A, Etienne J, Arnault F, Brault D, Noé L, Chuat J C, Galibert F
CHU Pitié-Salpêtrière, Paris, France.
Comp Biochem Physiol B Biochem Mol Biol. 1995 Jul;111(3):385-98. doi: 10.1016/0305-0491(95)00006-t.
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.
通过比对人、猪、牛、羊、小鼠、大鼠、豚鼠和鸡这八个物种中脂蛋白脂肪酶的核苷酸和氨基酸序列，我们发现主要结构域（催化结构域、N - 糖基化结构域和假定的肝素结合位点）高度保守。最长的相同氨基酸链由外显子2末端和外显子3起始处之间的序列编码，这突出了该区域的重要性，该区域除了其他结构域外，还编码活性位点的β5环。外显子10在我们研究的七种哺乳动物中完全不翻译，并且包含物种特异性的缺失、插入或富含A或A + T的元件。在鸡中，外显子10的起始部分被翻译。这八个先前未报道的比对结果可能是进一步研究LPL功能的有用工具。
