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fattyacids, ncbi, fatty infiltration of liver , fat girls , fat girls pics , big and plump , heird, research, all creatures, galland, hepatitis a, distilled water, science, ucdavis nutrition department, breaking, girls with fat ass , | (MBP) that fat plump represent the loading unit, 3 fatty acid chain elongation modules, and a terminating unit. The enzymatic activity within the 3 elongation modules is being assayed using various protocols. Up to date, we have determined the activities of ketoacyl synthase (KS) and enoyl reductase (ER). The activities of other enzymes within the three modules are currently being fat plump assayed. In addition, we have shown that the CpFAS1 KS fat plump activity can be inhibited by cerulenin, and its 50% inhibition concentration (IC50) is also determined. 2. We have identified another giant protein belonging to the fatty acid/polyketide synthase superfamily from C. parvum (CpPKS1), which contains a 40-kb open reading frame (ORF) encoding at least 29 individual enzymatic domains. |
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The proposed research will: 1) greatly expand our basic understanding of the biology of these apicomplexan parasites at molecular and biochemical level, and 2) provide potential molecular targets for fat girls pics the drug development against cryptosporidisis and/or coccidiosis. KEYWORDS: apicomplexan; parasite; cryptosporidium parvum; cryptosporidiosis; eimeria tenella; coccidiosis; energy metabolism; fatty acid biosynthesis; fatty acid synthases; glycolytic pathway; membrane transporters; p-type atpases; dna replication proteins; fat girls pics dna binding proteins; protein dna interaction; transcriptional coactivator; drug development PROGRESS: 2001/01 TO 2001/12 1. We have cloned and characterized a 25-kb multifunctional fatty acid synthase (FAS) fat girls pics from Cryptosporidium parvum (CpFAS1). This giant protein contains at least 22 enzymatic domains involved in the precursor-loading, 3 cycle of elongation of fatty acid 2-carbon (C2) units, and product-releasing. To further study and confirm the function of CpFAS1, as well as to validate whether CpFAS1 can be targeted by known inhibitors, we have constructed and expressed this protein as 5 individual recombinant proteins fused in a maltose-binding protein |
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