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  • 1
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0584
    Keywords: Thrombin-antithrombin III complex ; Prothrombin fragment 1+2 ; Blood withdrawal technique ; Catheter ; Venipuncture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To evaluate the influence of different blood sampling techniques on test results of thrombin-antithrombin III complex (TAT) and prothrombin fragment 1+2 (F1+2) serial determinations were performed. In six groups of nonrandomized patients (ten patients each) the concentrations of the coagulation markers of blood samples from central catheters (internal jugular, caval, Shaldon, pulmonary artery) and peripheral cannulas (17G and 18G) were compared with those of blood samples obtained simultaneously from direct venipunctures of the contralateral arm. Medians and 25th–75th percentiles of TAT and Fl+2 concentrations of plasmas obtained from central catheters were not different from those taken from venipunctures. When Δ mean values (catheter — venipuncture) were calculated negative results were obtained, indicating lower concentrations measured from blood sampled through central catheters with the exception of blood that taken from Shaldon catheters. Only for TAT concentrations significantly were lower values measured in blood samples taken from internal jugular catheters when compared with blood samples obtained from direct venipunctures. Significantly higher TAT concentrations were determined in blood samples obtained from Shaldon catheters. For both coagulation markers correlations were found between concentrations in blood samples from central catheters and venipunctures. In blood samples taken from peripheral venous cannulas only F1+2 concentrations correlated with the concentrations found in samples from direct venipuncture. In contrast to F1+2, TAT concentrations measured from blood samples via peripheral cannulas were determined significantly higher than those taken from direct venipunctures. Blood drawn from peripheral catheters is not suited for the determination of TAT and F1+2 due to frequently encountered activation of coagulation, while blood sampling with central catheters can be regarded as an alternative to venipuncture.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0584
    Keywords: Intracoronary stenting ; Aggressive anticoagulation ; Subacute occlusion ; Bleeding complication ; Prothrombin fragment 1+2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Patients with intracoronary stent implantation are treated with aggressive anticoagulant and antiplatelet therapy consisting of high-dose heparin, phenprocoumon, acetylsalicylic acid, dipyridamole, and the infusion of dextran to prevent a subacute thrombotic occlusion of the stented segment. In an effort to optimize this treatment by reducing both imminent bleeding complications and subacute thrombotic occlusion, the concentrations of prothrombin fragment 1+2 (F1+2) were determined after intracoronary Palmaz-Schatz stent implantation in 19 consecutive patients. The F1+2 concentrations after stent implantation and before the initiation of oral anticoagulant therapy (OAT) were 0.35 nm/l and 0.25–0.53 nm/l (median and 25th–75th percentile), versus 0.74 nm/l and 0.52–0.78 nm/l, in healthy subjects and 0.61 nm/l and 0.30–1.02 nm/l in 15 patients with ongoing proximal DVT. Nine days after initiation of OAT, F1+2 concentrations in both patient groups had not yet reached levels observed in patients with OAT in the stable state (0.16 nm/l, 0.12–0.26 nm/l;n=76;P〈0.0001 compared with healthy subjects; INR 2.0–4.5). Despite an INR greater than 2.0, accompanying heparinization was terminated on day 9. In two stented patients a minor bleeding complication arose after the removal of the arterial catheter. Subacute thrombotic occlusions were not observed. Since F1+2 concentrations did not exceed the upper limit of normal range (1.11 nm/l) in any of the 19 patients, the therapeutic regimen was not changed. Monitoring F1+2 may thus be helpful in introducing a more individual treatment if aggressive anticoagulation has to be performed.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1238
    Keywords: PMN-elastase ; Thrombin-antithrombin III-complex (TAT) ; Acute dialysis ; Low molecular weight heparin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Despite the improvements in the development of dialyzer membranes with greater hemocompatibility, an activation of the coagulation system occurs when blood comes into contact with exogenous surfaces. The large number of heparin dosage regimens demonstrate the difficulty to adapt general therapeutic guidelines. Low molecular weight heparin (Fragmin®) was administered as a single bolus dose for anticoagulation during 58 acute dialyses. Anti-Xa-activity, the plasma levels of the lysosomal elastase of the polymorphnuclear granulocytes (“PMN-elastase”) and of the thrombin-antithrombin III-complex (TAT) were measured at hourly intervals. Therapeutic anti-Xa-levels did not show evidence of sufficient inhibition of thrombin formation. The PMN-elastase increased by 180 ng/ml 3 h after administration of the bolus dose, with no further increase occurring (plateau phase). This was considered to reflect adequate anticoagulative activity. Where anticoagulation was inadequate, the elastase values rose consistently. After 2 h the increase of the PMN-elastase showed that — and to what extent — coagulation had been activated. The determination of PMN-elastase, using the IMAC-principle, is a method which can be performed quickly with any conventional autoanalyzer. It makes it possible to monitor adequate anticoagulation, but PMN-elastase results must be proven during routine use before recommendation as a routine test.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 43 (1965), S. 780-783 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Zusammenfassung Bei 31 Patienten mit entzündlichen und degenerativen Gelenkkrankheiten wurde im Serum und in der Gelenkflüssigkeit die Konzentration cinzelner Eiweißkörper untersucht. Es wurden bestimmt: Haptoglobin, Caeruloplasmin, sowie — mit der zweidimensionalen Agargeldiffusion nach Ouchterlony Transferrin, α2-Makroglobulin und α1-Seromucoid. Haptoglobin und Caeruloplasmin waren in der Synovia fast stets schwächer, α1-Seromucoid vorwiegend stärker vertreten als im Serum. Bei Transferrin und α2-Makroglobulin waren die Relationen Synovia/Serum nicht einheitlich. Wahrscheinliche Bedingungen dieser Unterschiede zwischen Serum und Erguß werden diskutiert.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 43 (1965), S. 27-30 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary The normal urinary excretion of ketopentoses during a period of 12 hrs is found to be in the range of 1 to 7 mg. The direct colorimetric assay of ketopentoses in the urine with cysteine-carbazol gives to high values due to unidentified cysteine-carbazol positiv material. Only by column chromatography and paper chromatography reliable data can be obtained. After intravenous injection of 20 g xylitol only in 5 out of 9 cases a slight increase in ketopentose excretion can be found. After oral administration of 20 g D-xylose there is a roughly 100fold increase in ketopentose excretion, consisting of D-xylulose and ribulose. It is assumed that this increase in ketopentose excretion is the result of an inhibition of transketolase by xylose. Frl.Käthe Wagner danken wir für stets zuverlässige technische Assistenz.
    Notes: Zusammenfassung Die Ausscheidung an Ketopentosen im normalen 12 Std-Harn liegt in der Größenordnung von 1–7 mg. Eine direkte quantitative Bestimmung dieser Ketopentosen mit der Cystein-Carbazol-Reaktion ist nicht möglich, da durch nichtidentifizierte Cystein-Carbazolpositive Substanzen zu hohe Werte vorgetäuscht werden. Nur Säulenchromatographie und papierchromatographische Analyse kann zuverlässige Werte liefern. Nach intravenöser Belastung mit 20 g Xylit wird bei 5 von 9 Fällen ein geringfügiger Anstieg der Ketopentose-Ausscheidung gefunden. Nach oraler Belastung mit 20 g D-Xylose steigt die Ketopentose-Ausscheidung im Harn auf etwa das 100fache der Norm an. Es handelt sich um D-Xylulose und Ribulose. Als Ursache für diese vermehrte Ausscheidung an Ketopentosen wird eine Hemmung der Transketolase durch Xylose angenommen.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 44 (1966), S. 989-998 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Sera of γ1A, γ1M and γSS paraproteins were subjected to gel filtration on sephadex G200 before and after treatment with cysteamine. The fractions obtained were examined by ultrazentrifugation and by immunological methods. The second fraction after gelfiltration before and after cysteamine treatment were rechromatographed on sephadex DEAE and TEAE. The subfractions obtained by this procedure were examined by ultrazentrifugation, immunological methods and by starchgel-electrophoresis. Cysteamine treatment causes splitting off of a globulin from fraction I after gelfiltration with S=6 to 7×1013. This component is eluted with the fraction II due to its low molecular weight. According to the agar diffusion test the split off globulin behaves like an atypical γ1A globulin. From the γ1 macroglobulin an immunological active γ1M globulin is splitt off by cysteamine. This has a sedimentation constant of S=6.34×10−13 and is eluted with the fraction II. The second fractions after gelfiltration of sera before and after cysteamine treatment show different chromatographic patterns on sephadex DEAE and TEAE, both, quantitatively and qualitatively. It is concluded, that this is caused by a chenged primary structure of the paraproteins compared to normale globulins. There are also differences in the chromatographic patterns of sera from different patientes. The compounds after sephadex DEAE and TEAE chromatography do not differ in their sedimentation constants but they prove to be heterogenous in starchgel-electrophoresis. So far the individual specifity of the paraproteins is proved.
    Notes: Zusammenfassung Die Seren von γ A-, γ M- und γ G-Paraproteinen wurden vor und nach Behandlung mit Cysteamin an Sephadex G200 gelfiltriert. Die erhaltenen Fraktionen wurden sedimentationsanalytisch und immunologisch untersucht. Die II. Fraktionen nach Gelfiltration vor und nach Cysteamin wurden an den Anionenaustauschern Sephadex DEAE und TEAE rechromatographiert. Die so erhaltenen Unterfraktionen wurden ebenfalls sedimentationsanalytisch, immunologisch und in der Stärkegelelektrophorese untersucht. Durch das Cysteamin wird bei den γ A-Paraproteinen aus der I. Fraktion nach Gelfiltration ein Globulin mit der Sedimentationskonstanten S=6 bis 7×10−13 abgespalten, das auf Grund des geringeren Molekulargewichtes in der II. Komponente eluiert wird. Bei dem abgespaltenen Globulin handelt es sich nach dem Agardiffusionstest um ein atypisches γ A-Globulin. Bei den γ-Makroglobulinen wird durch Cysteamin aus der I. Fraktion nach Gelfiltration ein immunologisch aktives γ M-Globulin abgespalten, das eine Sedimentationskonstante S=6,34×10−13 aufweist und in der II. Komponente eluiert wird. Die Rechromatographie der II. Fraktionen nach Gelfiltration vor und nach Behandlung der Seren mit Cysteamin an Sephadex DEAE und TEAE zeigt gegenüber der Norm ein in quantitativer und qualitativer Hinsicht abweichendes Bild. Daraus wird auf eine veränderte Primärstruktur der Paraproteine geschlossen. Auch untereinander weichen die Chromatogramme der untersuchten Seren deutlich voneinander ab. Diese Komponenten nach Rechromatographie an Sephadex DEAE sind größtenteils in bezug auf die Sedimentationskonstante einheitlich, in der Stärkegelelektrophorese sind die Komponenten heterogen. Damit ist die Individualspezifität der Paraproteine erneut belegt.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 43 (1965), S. 1209-1215 
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Four different proteines, humane- and bovine albumine, bovine γ-globuline and ovalbumine were irradiated in aqueous solution with 0,1–20 Mrad in an electrone accelerator Typevan de Graaf. After this treatment we analysed the change of pH, of the light scattering at 325 µm, of the isoelectric point, of the UV spectrum, of the proteine-N and non-proteine-N, of the aminoacid compound, of the relative viscosity, of the proteine bound glucose and neuramine acid and of the electrophoretic, and chromatographic behaviour an Sephadex DEAE. Increasing the dose of radiation, we found an increase of denaturation and of relative viscosity. The isoelectric point was altered, the proteine-N and the α-amino-N decreased, the non-proteine-N increased, free NH3 was formed. The proteine bound glucose and neuramine acid were partly splitted. The electrophoretic and chromatographic behaviour intensely altered, based on the increase of viscosity and alteration of electric charge.
    Notes: Zusammenfassung Vier verschiedene Proteine, Human- und Rinderalbumin, γ-Globulin vom Rind und Ovalbumin wurden in wäßriger Lösung mit 0,1 bis 20 Mrad im Elektronenaccelerator bestrahlt. Untersucht wurden die Veränderungen des pH, der Lichtstreuung bei 325 µm, des isoelektrischen Punktes, der UV-Spektren, des Protein-N und Nicht-Protein-N, der Aminosäurenzusammensetzung, der relativen eiweißgebundenen Glucose und Neuraminsäure und das elektrophoretische und chromatographische Verhalten an Sephadex DEAE. Mit steigender Strahlendosis kommt es zu einer zunehmenden Denaturierung der Proteine mit Zerstörung der Tertiärstruktur. Die relative Viscosität steigt an, es kommt zu einer Verschiebung des isoelektrischen Punktes. Der Protein-N-Gehalt, der α-Aminosäure-N nimmt ab, der Nicht-Protein-N steigt an, es kommt zur Bildung von freiem NH3. Die eiweißgebundene Glucose und Neuraminsäure werden z.T. abgespalten. Die elektrophoretische Wanderung und das chromatographische Verhalten ändern sich stark auf Grund der Viscositätszunahme und der Veränderung der elektrischen Ladung.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Four different proteines, humane — and bovine albumine, bovine gamma-globuline and ovalbumine were irradiated in aqueous solution with 0,1—30 Mrad in an electron accelerator typevan de Graaf. From these treated proteines we determined the Michaelis-constants of pepsine and trysine according toLineweaver andBurk. Up to the dosis of 5 Mrad we found with humane and bovine albumine a decrease of the constants of both encymes, increasing the dosis of radiation the constant ascended. In contrast of these results, the constants of pepsine and trypsine increased with bovine gamma globuline and ovalbumine as early as the dosis of 0,1 Mrad. Moreover we analysed the fragments of the irradiated proteines formed by hydrolysis with pepsine by agarelectrophoresis and chromatography on Sephadex G 25. With humane and bovine Albumine we found up to the dosis of 5 Mrad an increase of low-molecular fragments, they decreased after treatment with 10–30 Mrad. The bovine gamma globuline show a decrease of the low molecular fragments in favour of the non hydrolysed proteine at the dosis of 1 Mrad.
    Notes: Zusammenfassung Vier verschiedene Proteine, Human- und Rinderalbumin, γ-Globulin vom Rind und Ovalbumin wurden in wäßriger Lösung im Elektronenaccelerator nachvan de Graaf mit 0,1 bis 30 Mrad bestrahlt. Von den so verschieden behandelten Eiweißen untersuchten wir die Michaelis-Konstanten des Pepsins und Trypsins nachLinewaever undBurk. Bei dem Human- und Rinderalbumin kommt es bis zu einer Strahlendosis von 5 Mrad zu einem Abfall derK m -Werte beider Enzyme, bei höheren Dosen zu einem deutlichen Anstieg. Bei dem γ-Globulin und Ovalbumin steigen schon bei 0,1 Mrad die Michaelis-Konstanten an. Daneben untersuchten wir agarelektrophoretisch und chromatographisch an Sephadex G 25 die durch Pepsin entstandenen Bruchstücke der einzelnen Proteine. Dabei kommt es beim Human- und Rinderalbumin bei niederen Strahlendosen zu einer Zunahme der niedermolekularen Fragmente, bei höheren Dosen nehmen sie ab. Bei dem γ-Globulin sehen wir schon bei 1 Mrad eine Abnahme der hydrolysierten Bruchstücke zugunsten des nicht gespaltenen Eiweißes.
    Type of Medium: Electronic Resource
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