Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.6 (thromboplastin)
 13,278 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To measure the follow-up costs of preoperative coagulation screening tests, the authors studied 829 consecutive patients undergoing inpatient orthopedic surgery. The results of the initial prothrombin and activated partial thromboplastin time tests were divided into three groups: normal; abnormal above the hospital laboratory's upper limit of normal but below an "action limit"; and abnormal above an action limit. Patients with abnormal preoperative coagulation screening test results were matched on the basis of operative procedure and age with patients who had normal results. The matched groups of patients were compared according to preoperative length of stay and the cost of subsequent related preoperative testing. The average cost of follow-up preoperative testing for patients with abnormal screening test results was $5.05, compared with $0.58 for patients with normal screening results. The difference in average preoperative lengths of stay was not statistically significant. The attributable cost of evaluating an abnormal result added 3% to the cost of the initial coagulation screening program. This represents an average preoperative cost of $0.36 per patient in addition to the cost of the screening tests themselves.
J Gen Intern Med
PMID:Pursuit of abnormal coagulation screening tests generates modest hidden preoperative costs. 258 57

Adult male rats were subjected to intraperitoneal (i.p.) saline (controls) or barbiturates (20 mg/rat) as a single injection. Seventeen hours later the rats were sacrificed and plasma collected. Hematocrit (HCT), Platelet count (PLT), prothrombin time (PT), partial thromboplastin time (APTT), and coagulant activity for factors II, V, VII, VIII, X and XII, plus fibrinogen were determined. The data indicates that a single injection of phenobarbital and secobarbital had a greater effect on clotting activity than did barbital or amobarbital. This was primarily reflected in the hepatic synthesized clotting factors, plus the platelets.
Gen Pharmacol 1983
PMID:Clotting activity in the rat following acute barbiturate treatment. 664 93

To determine the adequacy of initial anticoagulation by intravenous heparin for patients who have deep venous thrombosis (DVT), and the factors that influence delayed anticoagulation, independent, duplicate chart review of 63 consecutive patients who had venography-proven DVT was conducted. Adequate heparinization (AH) was defined as an activated partial thromboplastin time (PTT) of more than 1.5 times the normal laboratory control. The proportions of patients achieving AH within 24 hours and 48 hours of initial heparin bolus were 46% and 62%, respectively. Patients who weighed more were less likely to achieve AH (p < 0.05), while patients receiving care from the thromboembolism service were more likely to achieve AH (p < 0.05). Low initial infusion rate was strongly but not significantly predictive of inadequate anticoagulation (p = 0.06). The mean heparin bolus and initial infusion rates were significantly lower than those suggested in the literature (p < 0.01). The AH rates were comparable to historical controls but suboptimal compared with the rates of 66% at 24 hours and 81% at 48 hours reported in association with heparin nomogram use (p < 0.05). A heparin nomogram is likely to achieve consistently higher rates of adequate heparinization.
J Gen Intern Med 1995 Jun
PMID:Inadequacy of intravenous heparin therapy in the initial management of venous thromboembolism. 756 29

1. We compared the low molecular weight heparinoid KB-101 and heparin with regard to suppression of experimental thrombus formation and effects on bleeding time, prothrombin time (PT), and activated partial thromboplastin time (APTT) in rats. 2. KB-101 exerted a similar antithrombotic activity as that of heparin. 3. Heparin prolonged bleeding time, PT, and APTT more than KB-101 did. 4. These results suggested that KB-101 is superior to heparin as an anticoagulant.
Gen Pharmacol 1993 Mar
PMID:Comparison of the antithrombotic effects of low molecular weight heparinoid KB-101 and heparin in a rat experimental model. 838 51

The gene encoding the envelope glycoprotein of a recent Danish isolate of a salmonid rhabdovirus, viral haemorrhagic septicaemia virus (VHSV) has been cloned and sequenced at the cDNA level. When compared with the deduced sequence of a French isolate of VHSV, it was noted that there were 13 amino acid substitutions in the Danish virus. Amino acid homologies with the glycoprotein of a North American salmonid rhabdovirus (infectious haematopoietic necrosis virus) indicate a high degree of structural similarity between the two fish rhabdovirus glycoproteins. Results from partial enzymatic deglycosylation of the viral protein indicate that all four NXT/S sites found in the sequence are N-glycosylated in the virus. The glycoprotein, without the N-terminal leader sequence and C-terminal hydrophobic anchor segment, was expressed in Escherichia coli as a factor Xa protease-cleavable fusion protein. The purified and renatured viral part of the recombinant protein was able to elicit VHSV-specific antibodies and neutralizing antibody activity in serum when injected into rainbow trout.
J Gen Virol 1993 Apr
PMID:Molecular cloning and expression in Escherichia coli of the glycoprotein gene of VHS virus, and immunization of rainbow trout with the recombinant protein. 846 53

The heat-stable enterotoxin b gene (estB) of Escherichia coli was fused to the gene for maltose-binding protein (malE). The estB gene was cloned into the pMAL-p vector using PCR. The construct consists of the signal sequence of maltose-binding protein, which directs the export of the fusion protein to the periplasm, and the maltose-binding protein fused to the STb polypeptide. A sequence encoding a factor Xa cleavage site is present between malE and estB. The fused genes are controlled by Ptac, a strong inducible promoter. Following IPTG induction, the recombinant strain expressed a 47 kDa protein, which was easily purified from osmotic shock fluid by using preparative electrophoresis and electroelution. Cleavage of the fusion protein with factor Xa generated the maltose-binding protein (42 kDa) and a polypeptide of approximately 5 kDa, corresponding to the molecular mass of mature STb. A monospecific polyclonal rabbit antiserum raised against purified STb reacted in immunoblot with the fusion protein and the cleaved-off peptide. A positive response was observed when testing the osmotic shock fluid containing the fusion protein in a rat intestinal loop assay. On average, 3-4 mg of MBP-STb protein was recovered per litre of induced recombinant strain.
J Gen Microbiol 1993 Mar
PMID:Fusion of the genes encoding Escherichia coli heat-stable enterotoxin b (STb) and the maltose-binding protein to obtain mature STb enterotoxin. 847 69

1. Effects of plancinin, a new anticoagulant peptide, on the human blood coagulation cascade were investigated. 2. Plancinin prolonged both activated partial thromboplastin time and prothrombin time, and it significantly inhibited factor X activation by both intrinsic (factor IXa-factor VIIIa-phospholipids-Ca2+) and extrinsic (factor VIIa-tissue factor-phospholipids-Ca2+) tenase complexes and prothrombin activation by prothrombinase complex (factor Xa-factor Va-phospholipids-Ca2+) to 13.8%, 4.8% and 10.5% of control value, respectively. 3. Results indicate that sites of anticoagulant action of plancinin may be located in activation steps of prothrombin and factor X.
Gen Pharmacol 1998 Aug
PMID:Analysis for sites of anticoagulant action of plancinin, a new anticoagulant peptide isolated from the starfish Acanthaster planci, in the blood coagulation cascade. 968 72

1. In batch adsorptions with prothrombin solutions, hyflo was the weakest adsorbent, standard super-cel intermediate, and filter-cel strongest. Of these three grades of diatomaceous earth, hyflo has the smallest surface area per gram and filter-cel the largest. In parallel breakthrough experiments, a column of standard super-cel had a capacity almost six times that of a hyflo column. 2. After partial removal of impurities by diatomaceous earth, prothrombin preparations contained less thrombokinase, were more stable, and displayed less tendency to form thrombin "spontaneously." Thrombokinase (or its precursor) was removed from a preparation of prothrombin by passage through a filter cake of standard super-cel. The specific activity of the prothrombin was increased; and 62 per cent of the activity was recovered. 3. Prothrombin was adsorbed from an ammonium sulfate solution at pH 5.26 by columns of hyflo or standard super-cel. When eluted by phosphate solutions, the protein moved down the columns more readily at higher pH and higher concentration of phosphate salts, within the pH range 5.0 to 6.6, and within the phosphate range 0.1 to 1.0 M. 4. Thrombin was adsorbed on a column of standard super-cel at pH 5.11. As successive eluents passed through the column, the thrombin emerged between two bands of impurities. The specific activity of the thrombin was raised; and 83 per cent of the activity was recovered. 5. With a column of standard super-cel, and with a series of eluents within the pH range 5.1 to 6.3, total serum proteins were separated into four major bands. About 94 per cent of the protein was recovered.
J Gen Physiol 1955 Jul 20
PMID:Chromatography of blood-clotting factors and serum proteins on columns of diatomaceous earth. 1324 61

1. Crystallized soy bean trypsin inhibitor, at a concentration of 100 microg./ml., suppressed the production of thrombin from a mixture of prothrombin and blood thrombokinase. The experiment was performed in the presence of 0.011 M oxalate, in order to minimize the possibility of participation by accessory factors which require ionic calcium. The results are in accord with the view that thrombokinase is a trypsin-like enzyme. 2. When a solution of blood thrombokinase was centrifuged at 85,000 g for 120 minutes, almost all the activity remained in the supernate. This supernate activated the supernate from a prothrombin solution which had been similarly centrifuged. The activation of prothrombin by thrombokinase can proceed in the absence of material completely sedimentable in 120 minutes at 85,000 g. 3. An "accelerator" reagent was prepared by treating bovine serum with barium carbonate, and then passing the serum through a column of diatomaceous earth. This "accelerator" was used together with prothrombin, blood thrombokinase, Howell's cephalin, and calcium chloride to compose a five-reagent thrombin-producing system. In this system, no thrombin was produced without thrombokinase. On the other hand, thrombin was produced from prothrombin and thrombokinase, even when all the other reagents were omitted. When calcium was omitted, thrombokinase was able to function; but cephalin and the "accelerator" reagent were ineffective. 4. Quantitative tests indicated that the "accelerator" reagent exerted an effect distinct from those of thrombokinase and cephalin. However, it is not certain whether the "accelerator" reagent functioned as an accessory factor, as a potential source of more thrombokinase, or both. In the experiments reported, thrombokinase was primary to, or necessary for, the effect of "accelerator." 5. The effectiveness of thrombokinase was multiplied a hundred times or more, when complemented by calcium, cephalin, and "accelerator" reagent. Ionic calcium was a necessary component of this complementing system. This may help to explain why removal of calcium ions keeps blood fluid, even though thrombokinase, by itself, is little influenced either by calcium ions or by oxalate.
J Gen Physiol 1955 Jul 20
PMID:Effect of blood thrombokinase, as influenced by soy bean trypsin inhibitor, ultracentrifugation, and accessory factors. 1324 62

THROMBOKINASE IS PREPARED FROM BOVINE PLASMA BY A PROCEDURE INVOLVING: treatment with diatomaceous silica, adsorption on barium sulfate, flowing elution with two successive phosphate buffers, ammonium sulfate fractionation, "spontaneous" activation in concentrated solution, and isoelectric precipitation. The yield of nitrogen is 0.002 per cent, corresponding to 1.2 mg. protein per liter of plasma. When diluted back to the volume of parent plasma, and complemented by calcium plus cephalin, the product causes appreciable activation of prothrombin in 1 minute. Thus, the quantity of thrombokinase obtainable is compatible with a physiologic role. In the more complex system used for routine assay, thrombokinase can be supplied by crude plasma at a dilution of 1/500. In parallel tests, the product appears to be more active than its parent plasma, although it contains only 0.002 per cent of the nitrogen. However, the thrombokinase of the product has been activated, whereas the thrombokinase of the plasma is probably in an inactive precursor state. When diluted back to the volume of parent plasma, to a concentration of 0.2 microgram nitrogen per ml., thrombokinase can slowly activate prothrombin in the presence of oxalate, and without the addition of accessory factors. Activation of prothrombin in the presence of oxalate is faster with higher concentrations of thrombokinase.
J Gen Physiol 1959 Mar 20
PMID:Preparation of thrombokinase from bovine plasma. 1363 Nov 94


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