Molecular Cloning of the cDNA of LPL on Goose and the Phylogenetic Relationship in the Lipase Superfamily

Lipoprotein lipase (LPL) of Tianfu meat goose was cloned and sequenced using a RT-PCR approach. The nucleotide sequence covered 468 bp with an open reading frame of 155 amino acids. Alignment analysis indicated that the nucleotide sequences are highly conserved to other species studied including chicken, domestic guinea pig, house mouse, Norway rat, cattle, cow and goat, and the homologies are 92.38%, 73.32%, 73.90%, 75.20%, 72.95%, 71.61% and 73.06%, respectively. Topology prediction showed goose LPL including two N-linked glycosylation site Asn 187 and Asn 215 ; one catalytic triad (Asp 183 and His 268 ); one conserved heparin binding site (Arg 134 to Arg 137 , (RKNR)); eight cysteine residues (Cys 68 and Cys 94 ; Cys 119 and Cys138; Cys130 and Cys 133 ; Cys 285 and Cys 306 ) that are involved in four disulfide bridges; and one lipid-binding site (Trp 256 and Trp 257 (WW)). Furthermore, molecular phylogeny analyses have shown that LPL protein families were divided into two main evolution branches, one was the LPL-EL-HL branch, and the other was the PL-PLA1 branch.