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4.
Blood Coagul Fibrinolysis ; 7(4): 453-8, 1996 Jun.
Article in English | MEDLINE | ID: mdl-8839997

ABSTRACT

In a multicentric study the influence of heparinase (Hepzyme) was evaluated on activated partial thromboplastin time, thrombin clotting time and prothrombin time using the recombinant human tissue factor and synthetic phospholipid (phosphatidylcholine and phosphatidyl-serine reagent). Hepzyme itself does not have any influence on normal coagulation values of activated partial thromboplastin time (aPTT) and prothrombin time (PT) assays whereas thrombin clotting time was prolonged by 10% (n = 60). In patients treated with unfractionated heparin for recent deep vein thrombosis (n = 47), plasma levels of aPTT, PT and thrombin clotting time (TCT) returned to the normal range in 100%, 97% and 91% after treatment with heparinase, respectively. Plasma samples of patients on coumarin were spiked with 2IU heparin/ml (n = 40) and were treated with heparinase. aPTT returned to baseline levels in 97.5%, PT in 99% and TCT in 69% of the samples. Plasma samples of patients receiving both heparin and coumarin were treated with heparinase (n = 18). aPTT and TCT values were shortened substantially and displayed the prolongation due to the effect of oral anticoagulants. PT values in these patients were also shortened. Freezing of plasma samples after treatment with heparinase resulted in a prolongation of the coagulation times in 15% of PT, 7% of aPTT and not of TCT values. The results show that treatment of plasma samples with heparinase abolishes the effect of unfractionated and low molecular weight heparin in vitro and ex vivo in patients during simultaneous treatment with oral anticoagulants. The use of heparinase may be of significance in patients with concomitant treatment of heparin and oral anticoagulants.


Subject(s)
Partial Thromboplastin Time , Polysaccharide-Lyases/pharmacology , Prothrombin Time , Thrombin Time , Thromboplastin , Freezing , Heparin/administration & dosage , Heparin/therapeutic use , Heparin Lyase , Humans , Indicators and Reagents , Recombinant Proteins , Reference Values , Warfarin/therapeutic use
5.
Phys Rev D Part Fields ; 42(9): 3246-3248, 1990 Nov 01.
Article in English | MEDLINE | ID: mdl-10013215
6.
J Biol Chem ; 265(16): 9520-5, 1990 Jun 05.
Article in English | MEDLINE | ID: mdl-2345180

ABSTRACT

A radioiodinated, photoactivatable derivative of Salmonella minnesota Re595 lipopolysaccharide (LPS) was used to label LPS-binding proteins in 70Z/3 cells. The labeled proteins were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and visualized by autoradiography. 125I-Labeled-2-(p-azidosalycylamido)1,3'-dithiopropionamide S. minnesota Re595 LPS (125I-ASD-Re595) labeled a limited number of proteins. The most prominent of these had a apparent molecular mass of 18 kDa. Less prominent labeling of 25- and 28-kDa proteins was also seen. Labeling was saturated by 5 micrograms/ml 125I-ASD-Re595 and was inhibited by a 10-100-fold excess of unlabeled LPS or lipid A. Labeling was maximal within 30 min at 37 degrees C; much less labeling occurred at lower temperatures. The proteins labeled with 125I-ASD-Re595 appear to be on the surface of the cell, since they can be digested by trypsin and were found in the membrane fraction of the cell but not in the cytosol. Studies with competitive inhibitors suggested that the proteins bind to the lipid A region of the LPS molecule. Biologically inactive lipid A analogs were poor inhibitors of labeling, suggesting that the LPS-binding proteins could discriminate between active lipid A and inactive analogs. These studies suggest that the 18- and 25-kDa proteins bind specifically to the lipid A region of the LPS molecule and should be considered as candidates for a functional LPS receptor.


Subject(s)
Affinity Labels , Carrier Proteins/analysis , Cross-Linking Reagents , Lipopolysaccharides/metabolism , Azides , Binding, Competitive , Carrier Proteins/metabolism , Cell Line , Cell Membrane/analysis , Cytosol/analysis , Kinetics , Lipid A/metabolism , Lipid A/pharmacology , Molecular Weight , Photochemistry , Protease Inhibitors/pharmacology , Salmonella , Temperature , Trypsin/metabolism
8.
Opt Lett ; 13(4): 285-7, 1988 Apr 01.
Article in English | MEDLINE | ID: mdl-19745874

ABSTRACT

We demonstrate that the amount of self-phase modulation in a coherent optical transmission system grows more slowly for a phase-modulated than for an amplitude-modulated signal. Signal degradation is discussed in terms of variations in the spectral contents of the amplitude and phase modulations, and explicit analytical expressions are given for the linear modulation indices of phase and amplitude of phase-shift keying coherent transmission systems.

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