Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.5 (thrombin)
 33,306 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Semi-synthesis of cellulose sulfate sodium (Na-MCS) was carried out by sulfation of microcrystalline cellulose (MCC) with chlorosulfonic acid-dimethylformamide complex as sulfating agent. As shown by FT-IR, NMR spectroscopy, and elemental analysis, the sulfation occurred mainly at C6, partially at C2, and no substitution at C3. The substitution degree ranged from 1.10 to 1.70 and the average molecular weight is between 1.1 and 3.5 x 10(4)Da. The anticoagulant efficacy and its possible mechanism were investigated using in vitro, in vivo coagulation assays and amidolytic tests in comparison with heparin. Results indicated that Na-MCS exhibited higher anticoagulation activity based on activated partial thromboplastin time (APTT) assay and prolonged the thrombin time (TT) to a lesser extent than heparin. No effect was detected on the prothrombin time (PT). Subcutaneous administration of Na-MCS to mice increased the clotting time (CT) in a moderate dose-dependent manner with a longer duration. Na-MCS exhibited anticoagulation activity mainly by accelerating the inhibition of antithrombin III (AT-III) on coagulation factors FIIa and FXa in plasma.
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PMID:Preparation and anticoagulation activity of sodium cellulose sulfate. 1760 35

Food-grade production of recombinant proteins in Gram-positive bacteria, especially in LAB (i.e., Lactococcus, Lactobacillus, and Streptococcus), is of great interest in the areas of recombinant enzyme production, industrial food fermentation, gene and metabolic engineering, as well as antigen delivery for oral vaccination. Food-grade expression relies on hosts generally considered as safe organisms and on clone selection not dependent on antibiotic markers, which limit the overall DNA manipulation workflow, as it can be carried out only in the expression host and not in E. coli. Moreover, many commercial expression vectors lack useful elements for protein purification. We constructed a "shuttle" vector containing a removable selective marker, which allows feasible cloning steps in E. coli and subsequent protein expression in LAB. In fact, the cassette can be easily excised from the selected recombinant plasmid, and the resulting marker-free vector transformed into the final LAB host. Further useful elements, as improved MCS, 6xHis-Tag, and thrombin cleavage site sequences were introduced. The resulting vector allows easy cloning in E. coli, can be quickly converted in a food-grade expression vector and harbors additional elements for improved recombinant protein purification. Overall, such features make the new vector an improved tool for food-grade expression.
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PMID:Advanced Strategies for Food-Grade Protein Production: A New E. coli/Lactic Acid Bacteria Shuttle Vector for Improved Cloning and Food-Grade Expression. 3103 73