Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

In the rabbit the application of a non-lethal, sleep-inducing dose of bromisovalerianyl carbamide (0.5 g/kg body weight) causes an activation of the coagulation system. This activation is manifested by shortened thrombin and partial thromboplastin times and a decrease of fibrinogen concentration and Factor V activity. In contrast, pentobarbital sodium at a dose (62.5 mg/kg) which causes the same changes in arterial partial oxygen pressure and arterial pH does not influence the coagulation system. The bromocarbamide-induced changes in the coagulation system are not to be considered as a result of hypoxia and acidosis but seem to be caused by early endothelial and tissue lesions which result in the release of procoagulatory substances. In healthy test persons a single dose of 1.5 g bromisovalerianyl carbamide has no demonstrable influence on the system of hemostasis.
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PMID:The activation of intravascular coagulation by bromocarbamide. 1 52

Human alpha-thrombin, the thromboplastin activation product of prothrombin with high clotting and esterase activity, was produced from Cohn Fraction III paste. The procedure started with 0.4 to 3.2 kg of frozen paste and was completed in 2 or 3 days. Some 23 g of thrombin were recorded for 65 quantitated preparations made from 11 lots of Fraction III paste. These preparations were obtained at protein concentrations of 3.9 +/- 1.3 mg/ml with a yield of 340 +/- 110 mg/kg of paste, which represented 48 +/- 14% of the clotting potential extracted as prothrombin. They had specific clotting activities of 2.8 +/- 0.4 U.S. (NIH) units/microng of protein and titrated to 88 +/- 8% active with p-nitrophenyl-p'-guanidinobenzoate (NPGB). Those (N - 29) examined by labeling with [14C]diisopropyl phosphorofluoridate (iPr2P-F) and electrophoresing in sodium dodecyl sulfate (SDS)-polyacrylamide gels were found to contain only (N = 4) or predominantly alpha-thrombin (97 +/- 3%) and corresponding amounts of ists degradation product, beta-thrombin (2.6 +/- 3.1%). No plasmin(ogen), prothrombin complex factors (II, VII, IX, IXalpha, X, Xalpha), or prothrombin fragments were detected in representative preparations. As produced in 0.75 M NaCl, pH approximately 6, thrombin was stable for approximately 1 week at 4 degrees and for greater than 1 year at less than or equal to 50 degrees; freeze-dried thrombin stored at 4 degrees for greater than 1 year displayed stable clotting activity and no vial to vial variation, permitting its use for reference purposes. Human thrombin generated by Taipan snake venom activation was compared with that produced by rapid thromboplastin activation: after treatment with [14C]iPr2P-F, greater than 95% of the label in both thrombins migrated at the same rate during electrophoresis in SDS; identical pairs of NH2-terminal residues were released in three consecutive Edman degradation cycles.
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PMID:Human thrombins. Production, evaluation, and properties of alpha-thrombin. 1 8

The reaction between activated factor X (Xa) and its natural inhibitor (XaI) was accelerated in vitro by both sodium heparin and an heparinoid, which was about 3 times less potent than heparin. The s. c. administration in humans of 5,000 units of sodium and calcium heparin was followed by the detection of a plasma activity potentiating XaI. In the majority of subjects, the heparinoid was not effective. These observations indicate that the use of heparinoids should not be considered as an alternative to heparin in the prevention of thromboembolism.
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PMID:Comparison of a natural heparinoid with sodium and calcium heparin for their effect on the inhibitor of activated factor X. 6 74

Plasmin does not activate factor X into the enzyme--factor Xa. On the contrary, the enzyme inactivates factor X, rendering it incapable of conversion into factor Xa during incubation in 25% sodium citrate. After proteolysis by plasmin the prothrombin preparations contaminated with factor X lose their ability to generate thrombin. This ability is partially restored by an addition of factor X.
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PMID:[Inactivation of factor X by plasmin]. 15 77

The use of heparin sodium and warfarin sodium in the treatment of pulmonary embolus (PE), deep vein thrombosis (DVT) and thrombophlebitis (TP) was studied by a hospital pharmacy department. During a four-month period, the charts of 26 patients were audited for anticoagulant dosages used; laboratory test monitoring of anticoagulant dosage used; laboratory test minitoring of anticoagulant therapy; complications of, contraindications to, and patient compliance with anticoagulant therapy. These variables were evaluated on the basis of compliance with a written anticoagulant protocol. Initial doses of heparin sodium and warfarin sodium were acceptable in 43% of patients. Maintenance dosing with heparin sodium was acceptable in 89% of patients. Activated partial thromboplastin times (APTT) were ordered correctly for 65% of patients. APTTs were within therapeutic ranges in 31% of patients. The duration of heparin-warfarin overlap was possibly to definitely acceptable in 71% of patients. Prothrombin times were properly monitored in 50% of patients. Complications of anticoagulant therapy were evident in only one patient. There were a number of potentially serious diversions from the protocol. The pharmacy department planned to issue bulletins designed to correct the problems.
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PMID:Audit of anticoagulant therapy of pulmonary embolus, deep vein thrombosis and thrombophlebitis. 42 Feb 10

Two methods of calculating heparin infusion rates for patients with venous thrombotic disease were compared; one method was based on a one-compartment pharmacokinetic model, the other on patient weight. Sixty-eight patients with presumed thromboembolic disease were started on continuous i.v. heparin sodium (porcine) using an infusion pump. Patients were divided into two groups--the infusion rate of Group I was based on patient weight (77 units/kg/4 hrs) and the infusion rate of Group 2 was determined by a pharmacokinetic equation based on a one-compartment heparin model. Heparin effect was measured by an activated partial thromboplastin time (APTT). The initial heparin infusion rate for Group 1 (4,784 +/- 672 units/4 hrs) was significantly greater (p less than 0.039, two-sample t-test) than that for Group 2 (4,413 +/- 779 units/4 hrs), but the variances of the rates were not significantly different (p = 0.40, ratio of variance F-test). Both methods for estimating initial heparin infusion rates gave mean APTT values in the center of the therapeutic range, but the variance in the APTTs of Group 2 patients was significantly smaller (p = 0.004) than that of Group 1. The pharmacokinetic model was more precise and reliable. This model should be valuable for insuring heparin's therapeutic effect without exposing patients to the potential risk of hemorrhage.
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PMID:Improved methods for estimating initial heparin infusion rates. 46 94

Two hours before surgery and every 12 hours thereafter 5,000 units of heparin sodium was administered subcutaneously to 100 general surgical patients. Hemostasis was evaluated by a template bleeding time and an activated partial thromboplastin time (PTT). The latter was sensitive to 0.05 units/ml of heparin and gave a straight-line response up to 0.2 units/ml. In the great majority of patients, only a modest elevation of the PTT occurred two and four hours after heparin therapy. However, in 10% to 15% the PTT was prolonged two times or more and in a similar number, PTT after surgery was shorter than baseline values despite heparin. No correlation between PTT prolongation and weight, ponderal index, age, or sex was found. Significant bleeding occurrred in three patients, two from the group of hyperresponders to heparin. Recent aspirin ingestion was implicated in one patient and our evidence indicates that low-dose heparin potentiates aspirin-induced prolongation of bleeding time in certain individuals. Local hematoma formation and discomfort from the injections was not a problem.
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PMID:Hemostatic effects of uniform, low-dose subcutaneous heparin in surgical patients. 61 30

A study with chicks was conducted to compare the relative vitamin K3 stability of various menadione preparations in mash and pellets. The preparations assayed were menadione sodium bisulfite, menadione sodium bisulfite complex, menadione dimethylpyrimidinol bisulfite and Kastab (a physically stabilized preparation of menadione sodium bisulfite). Pelleting increased the stability of all preparations when measured by the partial thromboplastin assay. The general trend in stability obtained by both procedures was in decreasing order: Kastab, menadione dimethylpyrimidinol bisulfite, menadione bisulfite complex and menadione bisulfite. Stability, determined chemically in vitamin microelement premixes, gave similar results.
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PMID:Effect of pelleting on the vitamin K activity of various vitamin K3 preparations in chicks. 67 7

The results of sending specimens through a computerized pneumatic airtransport system and manually delivering specimens were compared for 15 chemical tests and six hematologic procedures. All specimens were collected from inpatients and outpatients into evacuated glass containers. The specimens traversed a maximum of 829 feet (253 meters) involving 16 bends and eight transfer units at 25 feet/second (7.6 meters/second). Only the activity of lactate dehydrogenase exceeded the precision of the test in pneumatically transported specimens. Ruptured erythrocytes in incompletely filled vacuum tubes were the likely source of the increased lactate dehydrogenase activity. Neither the serum sodium, potassium, chloride, carbon dioxide, total protein, albumin, calcium, glucose, creatinine, total bilirubin, alkaline phosphatase, aspartate transaminase, acid phosphatase, uric acid, leukocyte count, erythrocyte count, hemoglobin, hematocrit, nor the prothrombin time and partial thromboplastin time were affected by pneumatic transport. It is concluded that the pneumatic system tested provides a safe, efficient method of transporting the blood specimens tested.
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PMID:Evaluation of a computer-directed pneumatic-tube system for pneumatic transport of blood specimens. 70 6

Factor XII was purified approximately 14 000-fold from bovine plasma by ammonium sulfate fractionation followed by heparin-agarose, DEAE-Sephadex, CM-cellulose, arginine-agarose, and benzamidine-agarose column chromatography. By this method, about 15 mg of protein was purified from 15 L of plasma with an overall yield of 18%. The purified protein was homogeneous as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino-terminal analysis. Bovine factor XII is a glycoprotein with a mol wt of 74 000 as determined by sedimentation equilibrium centrifugation. It contains 13.5% carbohydrate including 3.4% hexose, 4.7% N-acetylhexosamine, and 5.4% N-acetylneuraminic acid. Factor XII is a single polypeptide chain with an NH2-terminal sequence of Thr-Pro-Pro-Trp-Lys-Gly-Pro-?-Lys-His. This sequence is homologous to the reactive-site regions of a number of protease inhibitors. The amino acid sequence of a carboxyl-terminal fragments prepared by cyanogen bromide digestion was found to be Leu-Cys-Ala-Gly-Phe-Leu-Glu-Gly-Gly-Thr-Asp-Ala-Cys-Gln-Gly-Asp-SER-Gly-Gly-Pro-Leu-Val-Cys-Glu-Asp-Glu. This sequence is homologous with the active site of a number of plasma serine proteases including thrombin, factor IXa, factor Xa, and plasmin. These data indicate that bovine factor XII is a precursor to a serine enzyme with an inhibitor sequence and a catalytic site located in the same single polypeptide chain.
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PMID:Isolation and characterization of bovine factor XII (Hageman factor). 86 Dec 10


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