scholarly journals Comparison of polymerization of ancrod and thrombin fibrin monomers

Blood ◽  
1977 ◽  
Vol 50 (4) ◽  
pp. 619-624
Author(s):  
GG Jr Spellman ◽  
JA Macoviak ◽  
HR Gralnick
Keyword(s):  
Ionic Strength ◽  
Potent Inhibitor ◽  
Inhibitory Effect ◽  
Fibrin Monomer ◽  
Thrombotic Complications ◽  
Protein Incorporation ◽  
Benzyltriethylammonium Chloride ◽  
Fibrin Monomers

The polymerization of thrombin and ancrod fibrin monomers was studied with a standardized technique that evaluated turbidity changes and protein incorporation into the clot. Ancrod fibrin monomers were found to polymerize more slowly and form less turbid clots (at identical protein concentrations). Changes in ionic strength and pH influences ancrod fibrin monomer polymerization to a greater extent than thrombin fibrin monomer polymerization. Benzyltriethylammonium chloride was shown to be a potent inhibitor of fibrin monomer polymerization, with a greater inhibitory effect on ancrod fibrin monomers than on thrombin fibrin monomers. The differences between ancrod and thrombin fibrin may play a role in the infrequent thrombotic complications reported with ancrod therapy.

scholarly journals Comparison of polymerization of ancrod and thrombin fibrin monomers

Blood ◽  
1977 ◽  
Vol 50 (4) ◽  
pp. 619-624 ◽  
Author(s):  
GG Jr Spellman ◽  
JA Macoviak ◽  
HR Gralnick
Keyword(s):  
Ionic Strength ◽  
Potent Inhibitor ◽  
Inhibitory Effect ◽  
Fibrin Monomer ◽  
Thrombotic Complications ◽  
Protein Incorporation ◽  
Benzyltriethylammonium Chloride ◽  
Fibrin Monomers

Abstract The polymerization of thrombin and ancrod fibrin monomers was studied with a standardized technique that evaluated turbidity changes and protein incorporation into the clot. Ancrod fibrin monomers were found to polymerize more slowly and form less turbid clots (at identical protein concentrations). Changes in ionic strength and pH influences ancrod fibrin monomer polymerization to a greater extent than thrombin fibrin monomer polymerization. Benzyltriethylammonium chloride was shown to be a potent inhibitor of fibrin monomer polymerization, with a greater inhibitory effect on ancrod fibrin monomers than on thrombin fibrin monomers. The differences between ancrod and thrombin fibrin may play a role in the infrequent thrombotic complications reported with ancrod therapy.

Polymerisation Defect of Fibrinogen London

1979 ◽  
Author(s):  
D.A. Lane ◽  
M. VanRoss ◽  
B. Cuddigan ◽  
V.V. Kakkar
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Fibrinopeptide A ◽  
Protamine Sulphate ◽  
Terminal Domain ◽  
Coagulation Defect ◽  
Fibrin Monomer ◽  
Ca Ions ◽  
Polypeptide Chains ◽  
Fibrin Monomers

In the present study further work has been carried out on fibrinogen that has been isolated from a patient with a coagulation defect tentatively designated fibrinogen London. The dysfibrinogenemia was characterised by normal polypeptide chains on SDS gel electrophoresis, normal release of fibrinopeptide A and a delayed polymerisation of fibrin monomers. The polymerisation defect was pH and ionic strength dependent and partially corrected by protamine sulphate and Ca++ ions. Studies on the NH2 and COOH terminal polymerisation domains were carried out using insolubilised fibrin monomers prepared from patient and normal fibrinogen (Kudryk et al, Thromb. Res, 9,25. 1976). High MW fragment D, prepared by plasmin digestion of normal fibrinogen, bound to both normal and patient fibrin monomer and was eluted with 8M urea indicating no gross malfunction of the NH2 terminal polymerisation domain. Also purified fibrinogens from normal and patient plasma a bound to normal fibrin monomer sepharose, suggesting that the COOH terminal domain is capable of binding to the NH2 terminal domain of normal fibrin. These results suggest that the polymerisation defect of fibrinogen London is different in character to that of fibrinogen Detroit, where the NH2 terminal domain does not bind to the normal COOH terminal domain.

The Mechanism Of Inhibition Of Fibrin Assembly By Fragment D

1981 ◽  
Author(s):  
J Williams ◽  
R Hantgan ◽  
D Knoll ◽  
J McDonagh ◽  
J Hermans
Keyword(s):  
Light Scattering ◽  
Ionic Strength ◽  
Inhibitory Effect ◽  
Scattering Data ◽  
Radius Of Gyration ◽  
Lateral Association ◽  
Negative Stain ◽  
Fibrin Monomer ◽  
Mechanism Of Inhibition ◽  
Fiber Thickness

Measurements of clot rigidity and fiber thickness indicate that fragment D is a potent inhibitor of fibrin assembly. At physiological ionic strength, D concentrations in excess of 2 moles D/mole fibrinogen lead to a large decrease in clot rigidity and fiber thickness. Above 14 moles D/mole fibrinogen, gelation is inhibited. The molecular weight and radius of gyration of the fibers, determined by light scattering, confirm that short oligomers result, composed of 3 fibrin monomer molecules at 120 moles D/mole fibrinogen and 9 monomers at 14.4 moles D/mole fibrinogen. If D is added to a solution of long protofibrils, no inhibition is observed. Apparently the polymerization of monomers to protofibrils is blocked by D, but not lateral association.Inhibition of protofibril growth was studied in 0.5 M NaCl, pH 7.4, where lateral association is limited by the ionic strength. Stopped-flow light scattering data show a small decrease in the initial rate of polymerization and a slightly prolonged t½ ; the final intensity is less than that for a solution of long protofibrils. This result suggests that fragment D binds to the growing protofibrils with a small effect on the initial polymerization rate, but exerts its inhibitory effect by limiting the later stages of protofibril growth. Measurements of the length of the inhibited protofibrils, calculated from diffusion coefficients obtained by dynamic light scattering, confirm that polymers containing as few as 15 monomers have been obtained. Negative stain electron microscopy also shows a clear limitation of polymer growth under these conditions.Fragment D interferes with fibrin formation by directly blocking the first assembly step: bimolecular polymerization of activated fibrin monomer molecules to form protofibrils. Fragment D apparently occupies a site normally occupied by a fibrin monomer molecule, thus forming a dead-end complex which cannot undergo further assembly.

A New Congenital Dysfibrinogenemia with Hemorrhagic Diathesis (Fibrinogen Montreal II)

1975 ◽  
Author(s):  
G. Angelo ◽  
M. Lacombe ◽  
J. Lemay ◽  
R. Lavallée ◽  
Y. Bonny ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Prothrombin Time ◽  
Autosomal Dominant ◽  
Inhibitory Effect ◽  
Heat Denaturation ◽  
Hemorrhagic Diathesis ◽  
Fibrinogen Concentration ◽  
Results Of Treatment ◽  
Caucasian Family ◽  
Fibrin Monomers

This report comprises of a new congenital dysfibrinogenemia in a Caucasian family with hemorrhagic diathesis.Based on a study of three generations it shows to be an autosomal-dominant hereditary transmission.The thrombin and the Reptilase time are prolonged, the prothrombin time and the partial thromboplastin slightly prolonged.The fibrinogen concentration is normal when tested immunologically spectrophoto-metrically or by the heat denaturation method.Abnormal aggregation of fibrin monomers, and low optical density polymerisation curve with a correcting effect whenever the ionic strength is decreased below 0.15 M.The patient’s plasma has no inhibitory effect on the coagulation of normal plasma or fibrinogen.Satisfactory results of treatment with fibrinogen during dental extraction will be presented.

scholarly journals The Effect of pH, Ionic Strength and the Presence of PbII on the Formation of Calcium Carbonate from Homogenous Alkaline Solutions at Room Temperature

Minerals ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 783
Author(s):  
Fulvio Di Lorenzo ◽  
Kay Steiner ◽  
Sergey V. Churakov
Keyword(s):  
Ionic Strength ◽  
Deep Understanding ◽  
Inhibitory Effect ◽  
Alkaline Solutions ◽  
Nucleation Kinetics ◽  
Experimental Conditions ◽  
Calcium Carbonates ◽  
Natural Systems ◽  
Geological Processes ◽  
System Variables

Precipitation of calcium carbonates in aqueous systems is an important factor controlling various industrial, biological, and geological processes. In the first part of this study, the well-known titration approach introduced by Gebauer and coworkers in 2008 s used to obtain reliable experimental dataset for the deep understanding of CaCO3 nucleation kinetics in supersaturated solutions over a broad range of pH and ionic strength conditions. In the second part, the effect of impurities, i.e., 1 mol% of Pb2+, was assessed in the same range of experimental conditions. Divalent lead has been shown to have an inhibitory effect in all ranges of the conditions tested except for pH 8 and low ionic strength (≤0.15 mol/L). Future investigations might take advantage of the methodology and the data provided in this work to investigate the effect of other system variables. The investigation of all the major variables and the assessment of eventual synergic effects could improve our ability to predict the formation of CaCO3 in complex natural systems.

scholarly journals Influence of mitochondria on phospholipid synthesis in preparations from rat liver

1973 ◽  
Vol 136 (3) ◽  
pp. 467-475 ◽  
Author(s):  
J. B. Roberts ◽  
F. L. Bygrave
Keyword(s):  
Rat Liver ◽  
Inhibitory Effect ◽  
Total Radioactivity ◽  
Phospholipid Synthesis ◽  
Low Concentrations ◽  
Absolute Requirement ◽  
Reconstituted System ◽  
Protein Incorporation ◽  
Very High ◽  
Cellular Phospholipid

1. The addition of mitochondria to an incubation system containing the soluble and microsomal fractions of rat liver enhances severalfold the incorporation of each of ethanolamine, phosphorylethanolamine and CDP-ethanolamine into phosphatidylethanolamine. 2. In the presence of microsomal, mitochondrial and soluble fractions, CDP-ethanolamine exhibits the greatest initial rate of incorporation (approx. 6nmol/h per mg of protein), being slightly faster than that of phosphorylethanolamine (approx. 5nmol/h per mg of protein). Incorporation of ethanolamine proceeds very slowly for the first 20min and only after 30min gives rates approaching those of the other two precursors. 3. By using a substrate ‘dilution’ technique it was shown that in the reconstituted system the affinity of each of the enzymes for their respective substrates is very high: 10μm for ethanolamine, 25μm for phosphorylethanolamine and 5μm for CDP-ethanolamine. 4. Isolation of the mitochondrial and microsomal fractions from the medium after incubation together with phosphorylethanolamine showed that about 70% of the total radioactivity was present in the microsomal fraction and about 30% in the mitochondria after only 20min. Similar experiments with ethanolamine as precursor revealed that after 20min only about 15% of the total radioactivity was present in the mitochondria but that after 40min about 30% was present in this fraction. 5. Heating and phospholipase treatment of mitochondria, but not freeze-thawing, eliminated the stimulatory effect of mitochondria on phospholipid synthesis. 6. The reconstituted system exhibits an absolute requirement for Mg2+(2mm gave maximal rates) and is inhibited by very low concentrations of Ca2+(100μm-Ca2+produced half-maximal inhibition with 3mm-Mg2+). Further addition of Mg2+overcame the Ca2+inhibition, suggesting that the inhibitory effect is readily reversible. 7. The concept that modification of the Mg2+/Ca2+ratio is a means of controlling the rate of cellular phospholipid synthesis is introduced.

scholarly journals Role of diamine oxidase during the treatment of tumour-bearing mice with combinations of polyamine anti-metabolites

1983 ◽  
Vol 212 (3) ◽  
pp. 895-898 ◽  
Author(s):  
A Kallio ◽  
J Jänne
Keyword(s):  
Diamine Oxidase ◽  
Potent Inhibitor ◽  
Specific Inhibitor ◽  
Inhibitory Effect ◽  
Tumour Cells ◽  
Adenosylmethionine Decarboxylase ◽  
Growth Inhibitory ◽  
Sequential Combination ◽  
Marked Accumulation

Treatment of mice bearing L1210 leukaemia with 2-difluoromethylornithine, a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17), produced a profound depletion of putrescine and spermidine in the tumour cells. Sequential combination of methylglyoxal bis(guanylhydrazone), an inhibitor of adenosylmethionine decarboxylase (EC 4.1.1.50), with difluoromethylornithine largely reversed the polyamine depletion and led to a marked accumulation of cadaverine in the tumour cells. Experiments carried out with the combination of difluoromethylornithine and aminoguanidine, a potent inhibitor of diamine oxidase (EC 1.4.3.6), indicated that the methylglyoxal bis(guanylhydrazone)-induced reversal of polyamine depletion was mediated by the known inhibition of diamine oxidase by the diguanidine. In spite of the normalization of the tumour cell polyamine pattern upon administration of methylglyoxal bis(guanylhydrazone) to difluoromethylornithine-treated animals, the combination of these two drugs produced a growth-inhibitory effect not achievable with either of the compounds alone.

Effect of creatine on contractile force and sensitivity in mechanically skinned single fibers from rat skeletal muscle

2004 ◽  
Vol 287 (6) ◽  
pp. C1589-C1595 ◽  
Author(s):  
Robyn M. Murphy ◽  
D. George Stephenson ◽  
Graham D. Lamb
Keyword(s):  
Ionic Strength ◽  
Creatine Phosphate ◽  
Inhibitory Effect ◽  
Muscle Performance ◽  
Direct Effects ◽  
Contractile Apparatus ◽  
Single Fibers ◽  
Beneficial Effects ◽  
Osmotic Balance ◽  
Cellular Water

Increasing the intramuscular stores of total creatine [TCr = creatine (Cr) + creatine phosphate (CrP)] can result in improved muscle performance during certain types of exercise in humans. Initial uptake of Cr is accompanied by an increase in cellular water to maintain osmotic balance, resulting in a decrease in myoplasmic ionic strength. Mechanically skinned single fibers from rat soleus (SOL) and extensor digitorum longus (EDL) muscles were used to examine the direct effects on the contractile apparatus of increasing [Cr], increasing [Cr] plus decreasing ionic strength, and increasing [Cr] and [CrP] with no change in ionic strength. Increasing [Cr] from 19 to 32 mM, accompanied by appropriate increases in water to maintain osmolality, had appreciable beneficial effects on contractile apparatus performance. Compared with control conditions, both SOL and EDL fibers showed increases in Ca2+ sensitivity (+0.061 ± 0.004 and +0.049 ± 0.009 pCa units, respectively) and maximum Ca2+-activated force (to 104 ± 1 and 105 ± 1%, respectively). In contrast, increasing [Cr] alone had a small inhibitory effect. When both [Cr] and [CrP] were increased, there was virtually no change in Ca2+ sensitivity of the contractile apparatus, and maximum Ca2+-activated force was ∼106 ± 1% compared with control conditions in both SOL and EDL fibers. These results suggest that the initial improvement in performance observed with Cr supplementation is likely due in large part to direct effects of the accompanying decrease in myoplasmic ionic strength on the properties of the contractile apparatus.

Microbial degradation of benzene, toluene, ethylbenzene and xylene isomers (BTEX) contaminated groundwater in Korea

2001 ◽  
Vol 44 (7) ◽  
pp. 165-171 ◽  
Author(s):  
S. W. Chang ◽  
H. J. La ◽  
S. J. Lee
Keyword(s):  
Potent Inhibitor ◽  
Inhibitory Effect ◽  
Contaminated Groundwater ◽  
Interaction Patterns ◽  
Contaminated Aquifer ◽  
Substrate Interaction ◽  
Substrate Degradation ◽  
Benzene Toluene ◽  
Xylene Isomers ◽  
Btex Compounds

A mixed culture derived from a gasoline-contaminated aquifer in Korea was enriched on toluene at 25°C. A study was conducted to characterize the substrate interaction of BTEX by toluene-enriched consortia and determine the effects of initial BTEX concentration on BTEX degradation. Substrate degradation patterns in individual aromatics were found to differ significantly from patterns for aromatics in mixtures. In the experiment of a single substrate, toluene was degraded fastest, followed by benzene, ethylbenzene, and the xylenes. In BTEX mixtures, degradation followed the order of toluene, ethylbenzene, benzene, and the xylenes. The studies conducting with toluene-enriched consortia evaluated substrate interactions by the concurrent presence of multiple BTEX compounds and revealed a range of substrate interaction patterns including no interaction, stimulation, inhibition, and cometabolism. The simultaneous presence of benzene and toluene were degraded with a slight inhibitory effect on each other. Ethylbenzene was shown to be the most potent inhibitor of BTEX degradation. p-xylene also inhibited the degradation of benzene, toluene, and ethylbenzene, whereas the presence of either benzene or toluene enhanced the degradation of ethylbenzene and the xylenes.

A Novel Dysfibrinogenemia with Abnormal γ-Chain(Fibrinogen Nagoya).

1979 ◽  
Author(s):  
Junki Takamatsu ◽  
Kanji Oqata ◽  
Tadashi Kamiya ◽  
Katsuo Koie ◽  
Takagi Takashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Inhibitory Effect ◽  
Chain Structure ◽  
Japanese Family ◽  
Electrophoretic Mobilities ◽  
Sds Page ◽  
History Of ◽  
The Difference ◽  
Fibrin Monomers ◽  
Major Defect

Six individuals in 3 generations of Japanese family had prolonged thrombin clotting time, but no history of hemorrhagic or thrombotic disease. Very low fibrinogen levels were obtained by thrombin clottable protein, while immunological procedures gave normal values of fibrinogen. The serum contained 40-80μg/ml of unclottable fibrinogen related antigens. The patients’ plasma had an inhibitory effect on the fibrin formation in normal plasma. Major defect of this fibrinogen was a delayed aggregation of fibrin monomers.On CM-chromatography (CM-52) of the S-carboxymethylated fibrinogen, three different γ-chains, named γx, γL and γR, were separated. They did not differ in their electrophoretic mobilities in SDS-PAGE, but were distinguishable in PAGE containing 8M urea. Moreover, the amino acid compositions and tryptic peptide mappings of each chain revealed a little difference from those of normal fibrinogen γ chains, suggesting the difference in amino acid substitution or oligosaccharide chain structure.Based on these findings, we designated this fibrinogen as fibrinogen Nagoya; its possible identity without other dysfibrinogenemia has not been excluded.

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