Brault D, Noé L, Etienne J, Hamelin J, Raisonnier A, Souli A, Chuat J C, Dugail I, Quignard-Boulangé A, Lavau M
Laboratoire de Biochimie et Biologie Moléculaire, Faculté de Médecine St-Antoine, Paris, France.
Gene. 1992 Nov 16;121(2):237-46. doi: 10.1016/0378-1119(92)90127-b.
A rat lipoprotein lipase (LPL)-encoding cDNA (LPL) has been entirely sequenced and compared to the sequences of all the LPL cDNAs reported in other species. As expected, high homology was found between the coding exons. The putative catalytic triad, Ser132, Asp156, His241, according to human numbering, is conserved in rat. As is the case in mouse, an Asn444 present in human LPL is also missing. The major divergences between human, mouse and rat LPLs were observed in the untranslated exon 10, where (i) the rat cDNA exhibits a 157-bp insertion and an 81-bp deletion relative to human; (ii) neither the B1 repeat nor the homopurine stretch reported in mouse can be recognized, and (iii) the rat cDNA displays several A+T-rich stretches.
