Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.16.2 (PCP)
 3,761 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The sphingolipid activator protein, saposin C (also termed SAP 2), was chemically synthesized, purified, and characterized. The fully protected 82-residue protein was synthesized by automated solid-phase methods, with multiple recoupling steps resulting in a high average coupling efficiency of 98.8%. The overall yield was estimated to be approx 40%. Deprotection and cleavage of the peptide from the resin was followed by folding in the absence of chaotropic agents at pH 8.5. The protein was purified by reversed-phase high pressure liquid chromatography (HPLC) and its purity determined by capillary electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The composition of the synthetic saposin C was determined by amino acid analysis. Its sequence was verified by Edman sequence analysis of overlapping peptide fragments generated by chymotryptic and Staphylococcus aureus V8 digestions. The sequence at the C-terminus was determined by digestion with carboxypeptidase P, followed by phenylthiohydantoin (PTH) derivitization and HPLC analysis of the released amino acid residues. Deglycosylated native saposin C appeared as a lower molecular-weight species than synthetic saposin C on SDS-PAGE. This has been explained by amino acid and C-terminal analysis showing native saposin C to be two amino acids shorter at the C terminus than a deduced sequence (from cDNA) previously published. Synthetic saposin C displayed 85% of full biological activity as determined by its ability to stimulate glucocerebrosidase activity in vitro: Synthetic and native saposin C increased glucocerebrosidase catalyzed hydrolysis of 4-methylumbelliferyl beta-D-glucoside by factors of 6.0 and 7.1, respectively. Furthermore, synthetic and native saposin C share similar K(act) values (0.5 and 1.5 microM respectively) indicating that they bind to glucocerebrosidase with similar affinities.
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PMID:Synthesis and characterization of a bioactive 82-residue sphingolipid activator protein, saposin C. 829 89

Evaluation of the value of the systolic pressure variations (SPV) under mechanical ventilation and of its components (delta down and delta up) in predicting fluid responsiveness in patients after coronary surgery by comparison with classic parameters. A prospective,randomized study, on 50 patients who underwent CABG surgery, in the early postoperative period (the first two hours). We assessed the following parameters: CO, CI, CVP, PCWP, SAP, DAP, MAP, SVP, delta down and delta up. The including criteria were: sinus rhythm, CI < or = 2,5 l/min/m2, PCP < 18 mmHg. All the patients underwent a fluid challenge (500 ml of colloids in 10 min). Three patients were excluded: 3 for a PCWP > 18 mm Hg, 1 for loosing the sinus rhythm and 1 for an early return in the OR for bleeding. After a new assessment of the same parameters the patients were divided in two groups: group A (28 pts) with a raise of CI > 15%, and group B (22 pts) with a CI variation < 15%. In each group was statistically analyzed the variation of each parameter. Results Both parameters provided by SPV analysis are able to predict the fluid responsiveness with a great accuracy: the positive predictive value of a SPV > 12 mmHg is above 92,85% and of a delta down > 5 mm Hg is above 96,42%; the negative predictive value of a SPV < or = 12 mmHg is above 90,90% and of a delta down = 5 mm Hg is above 95,45%. None of the "classic" pressure parameters (MAP, CVP, PCWP) used in hemodynamic assessment have revealed a statistical significant variation. The SVP method's parameters are superior to classic pressure parameters (MAP, CVP, PCWP) in predicting fluid responsiveness in patients after coronary surgery.
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PMID:[A comparison between systolic pressure variations under mechanical ventilation and classic pressure parameters in predicting fluid responsiveness in patients after coronary surgery]. 1692 20