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The complete coding sequences (CDS) of the RBP5 and RBP7 genes were amplified using the reverse transcriptase polymerase chain reaction (RT-PCR) method, and the deduced amino acid sequences of both genes were compared to human corresponding proteins.
The contigs assembling of RBP5 and RBP7 genes were performed as described by Wang et al.
As amplifying the CDS of RBP5 and RBP7 genes, RT-PCR was carried out using the cDNA template derived from reverse transcription of pig liver and skeletal muscle total RNAs, respectively.
Using the IMpRH panel, we mapped the porcine RBP5 being closely linked (two-point-analysis) to the microsatellite marker SW963 (29cR; LOD score 16.
Using the primer pairs of CDS PL and CDS PR of each gene (Table 1), 728 bp and 558 bp cDNA fragments of porcine RBP5 and RBP7 genes were amplified by RT-PCR.
Porcine RBP5 and RBP7 belong to intracellular lipid-binding proteins (iLBPs), which contain RBPs, CRABPs and fatty acid-binding proteins (FABPs).
The result demonstrates that porcine RBP5 and RBP7 amino acid sequences perfectly match the characteristics of iLBPs family which all have 10 [beta]-stands (A-J) and two [alpha]-helices to form the well characterized [beta]-barrel.
108] which is replaced by a His residue in both human RBP5 and RBP7.
The RT-PCR was performed to detect the porcine RBP5 and RBP7 genes' expression patterns in 12 tissues of adult Wzhishan pig.
In general, porcine RBP5 and RBP7 have different expression patterns.
517] of RBP5 were confirmed by digestion with enzymes Cac8I, Mwo I and Fnu4H I, respectively, and the others were confirmed by direct sequencing of PCR products.
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