The porcine gene for α₁-acid glycoprotein (ORM1) was localized to chromosome region 1q210→ q212 by fluorescence in situ hybridization. From this result and published gene mapping data, it was concluded that the syntenic group comprised of ORM1, IFNA1, and GRP78 in the human genome is also conserved in the pig.

We have obtained a partial cDNA and three BAC clones for the porcine insulin-like growth factor binding protein 1 gene (IGFBP-1). Results of fluorescence in situ and radiation hybrid (RH) mapping assigned this gene to porcine chromosome (SSC) 18q24-qter. We found two types of polymerase chain reaction-restrictionfragment-length polymorphisms (PCR-RFLP) in intron 2 by using FokI and AluI.

ABSTRACT. To investigate the structure of porcine genes involved in the beta-oxdation of fatty acid, we isolated the short-chain acyl-CoA dehydrogenase (SCAD), medium-chain acyl-CoA dehydrogenase (MCAD), and long-chain acyl-CoA dehydrogenase (LCAD) genes from the pig. The cDNA of SCAD, MCAD and LCAD genes were 1899 bp, 1835 bp and1704 bp long and coded for 413-aa, 422-aa and 430-aa precursor proteins, respectively. Three genes, SCAD, MCAD and LCAD were mapped to 14p16. Comparison of amino acid sequences deduced from nucleotide sequences of the three enzyme cDNAs revealed that the sequence similarity between human and porcine SCAD was 89.6%, that between human and porcine MCAD was 87.2%, and that between human and porcine LCAD was 89.5%. Alignment of amino acid sequences of the three enzymes showed that 81 amino acids were shared among the three enzymes and 163 were shared between the two enzymes, so that totally 55.6% of amino acids were conserved in these sequences (Fig. 1). All three sequences contained a conserved FAD binding site (shaded box) and the sequence specific to the acyl-CoA dehydrogenase (shadow box). Studies of several lines of mutagenesis have shown that the glutamate in the latter sequence is presumed to have a crucial role in the abstraction of an alpha-proton from the substrate in the dehydrogenase reaction [6]. Our results also showed that the glutamates at the 375th in SCAD, at the 384th in MCAD and at the 395th LCAD were conserved among these three enzymes.Biotinylated probes of the complete SCAD and MCAD cDNA were generated by incorporation of biotin-16 dUTP using a nick translation kit (Boehringer Mannheim) [9], while digoxigenin labeling system was used for localization of the LCAD gene. The metaphase spreads were prepared from the porcine white blood cells. The hybridization signals were visualized using FITC-labeled streptavidine/ biotinylated anti-streptavidin antibody and rhodaminelabeled anti-digoxigenin antibody. Chromosomes (Chrs) were counterstained with PI for FITC and DAPI for rhodamine. FISH performed with a porcine SCAD probe allowed us to map the SCAD gene to Chr 14p16.1-p23.2 (Fig. 2 A). The genes localized on Chr 14 so far reported in the pig formed syntenies on Chr 12 in human [1] and Chr 5 in mice [7]. The MCAD gene localized on Chr 1 in human [4] and on Chr 3 in mice [8] was found to be located on the long arm of Chr 6, 32.4-33 region (Fig. 2 B). On the other hand, the LCAD gene was localized on Chr 15q24.2-q26.3The intracellular distribution and depositions of fat are considered to be crucial factors in meat quality in the pig. Most fats in the pig are stored as fatty acid and triacyl glycerols in the fat tissues through several pathways of the lipid metabolism. In addition to the synthetic pathways, the fat content in the meat may be influenced by the degradation of fatty acid. Oxidative degradation of fatty acids, betaoxidation, consists of a repeating circuit of four sequential steps in which acyl-CoA dehydrogenases catalyze the first step. There are four enzymes ta...