Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hyperacute organ xenograft rejection can be prevented by removing anti-pig antibodies by extracorporeal absorption prior to transplantation. A novel recombinant absorber of anti-pig antibodies was developed by fusing the cDNA encoding the extracellular part of a mucin-type protein, P-selectin glycoprotein ligand-1, with an antibody Fc fragment cDNA, which upon coexpression with the porcine alpha1,3 galactosyltransferase carried the xenogeneic epitope, Galalpha1,3Gal (Liu J., Qian Y., Holgersson J., Transplantation 1997, 63, 1673-1682). The biochemical characterization of the mucin/Ig and its absorption efficacy compared with that of porcine thyroglobulin and Galalpha1,3Gal-conjugated beads are reported. The carbohydrate portion of the mucin/Ig constituted 43% of its molecular weight and the majority of the Galalpha1,3Gal epitopes were O-linked as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting following N-glycosidase F digestion. Gas chromatography-mass spectrometry of reduced and acetylated saccharides released by alpha-galactosidase treatment revealed that the fusion protein carried approximately 140 mol of terminal, alpha-linked galactose per mole protein. Based on the reduction in pig aortic endothelial cell cytotoxicity, Galalpha1,3Gal-substituted mucin/Igs on agarose beads were, on a carbohydrate molar basis, shown to be approximately 20 times more efficient than agarose-conjugated pig thyroglobulin, and approximately 5000 and 30,000 times more efficient than Galalpha1,3Gal-substituted agarose and macroporous glass beads, respectively. Structural features of the mucin backbone and its carbohydrate core saccharide chains determine the structural context, spatial orientation and spacing of Galalpha1,3Gal epitopes and are likely to explain the superior absorption efficacy of the recombinant mucin-type chimera.
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PMID:Multivalent Galalpha1,3Gal-substitution makes recombinant mucin-immunoglobulins efficient absorbers of anti-pig antibodies. 1258 48

Five lipases, namely, Candida antarctica (Novozyme-435), Mucor miehei (Lipozyme-IM), Pseudomonas sp. (PS-30), Aspergillus niger (AP-12), and Candida rugosa (AY-30), were screened for their effect on catalyzing the acidolysis of tristearin with selected long-chain fatty acids. Among the lipases tested C. antarctica lipase catalyzed the highest incorporation of oleic acid (OA, 58.2%), gamma-linolenic acid (GLA, 55.9%), eicosapentaenoic acid (EPA, 81.6%), and docosahexaenoic acid (DHA, 47.7%) into tristearin. In comparison with other lipases examined, C. rugosa lipase catalyzed the highest incorporation of linoleic acid (LA, 75.8%), alpha-linolenic acid (ALA, 74.8%), and conjugated linoleic acid (CLA, 53.5%) into tristearin. Thus, these two lipases might be considered promising biocatalysts for acidolysis of tristearin with selected long-chain fatty acids. EPA was better incorporated into tristearin than DHA using the fifth enzymes. LA incorporation was better than CLA. ALA was more reactive than GLA during acidolysis, except for the reaction catalyzed by Pseudomonas sp., possibly due to structural differences (location and geometry of double bonds) between the two fatty acids. In another set of experiments, a combination of equimolar quantities of unsaturated C18 fatty acids (OA + LA + CLA + GLA + ALA) was used for acidolysis of tristearin to C18 fatty acids at ratios of 1:1, 1:2, and 1:3. All lipases tested catalyzed incorporation of OA and LA into tristearin except for M. miehei, which incorportaed only OA. C. rugosa lipase better catalyzed incorporation of OA and LA into tristearin than other lipases tested, whereas the lowest incorporation was obtained using Pseudomonas sp. As the mole ratio of substrates increased from 1 to 3, incorporation of OA and LA increased except for the reaction catalyzed by A. niger and C. rugosa. All lipases tested failed to allow GLA or CLA to participate in the acidolysis reaction, and ALA was only slightly incoporated into tristearin when M. miehei was used.
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PMID:Acidolysis of tristearin with selected long-chain fatty acids. 1728 39

A gas chromatography-mass spectrometry (GC-MS) method was developed to simultaneously separate cholesterol, eight cholesterol oxidation products (COPs), and two conjugated linoleic acids (9-cis,11-trans-CLA and 10-trans,12-cis-CLA) and to evaluate their stability in a model system during heating. Among four capillary columns tested, an Equity-5 column with low-polar stationary phase provided better resolution within 30 min. A high-performance liquid chromatography method was also developed to determine cholesterol hydroperoxides by using a YMC C30 column with diphenyl-1-pyrenylphosphine as fluorescence reagent. No formation of COPs or degradation of cholesterol and CLAs occurred at 100 degrees C, but the levels of COPs rose drastically at 150 degrees C. The first-order rate of cholesterol degradation declined following a rise in CLA concentration. For 0-, 100-, and 500-microg/ml CLA levels, the formation profiles of 7-hydroxycholesterol, 7-ketocholesterol, and 5,6-epoxycholesterol at 150 degrees C were fitted as multiple first-order curves, whereas a single first-order model could adequately describe 7-hydroperoxycholesterol and cholestane-3beta,5alpha,6beta-triol formation. A CLA-to-cholesterol mole ratio of 0.49 was required to prevent cholesterol oxidation at 150 degrees C.
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PMID:Gas chromatography-mass spectrometry determination of conjugated linoleic acids and cholesterol oxides and their stability in a model system. 2011 71