The Effect of Dextran of Various Molecular Weight on the Coagulation in Dogs

1961 ◽  
Vol 06 (01) ◽  
pp. 015-024 ◽  
Author(s):  
Sven Erik Bergentz ◽  
Oddvar Eiken ◽  
Inga Marie Nilsson
Keyword(s):  
Molecular Weight ◽  
Body Weight ◽  
High Molecular Weight ◽  
Bleeding Time ◽  
Factor Vii ◽  
Low Molecular Weight ◽  
Factor V ◽  
Coagulation Mechanism ◽  
Coagulation Defects

Summary1. Infusions of low molecular weight dextran (Mw = 42 000) to dogs in doses of 1—1.5 g per kg body weight did not produce any significant changes in the coagulation mechanism.2. Infusions of high molecular weight dextran (Mw = 1 000 000) to dogs in doses of 1—1.5 g per kg body weight produced severe defects in the coagulation mechanism, namely prolongation of bleeding time and coagulation time, thrombocytopenia, pathological prothrombin consumption, decrease of fibrinogen, prothrombin and factor VII, factor V and AHG.3. Heparin treatment of the dogs was found to prevent the decrease of fibrinogen, prothrombin and factor VII, and factor V otherwise occurring after injection of high molecular weight dextran. Thrombocytopenia was not prevented.4. In in vitro experiments an interaction between fibrinogen and dextran of high and low molecular weight was found to take place in systems comprising pure fibrinogen. No such interaction occurred in the presence of plasma.5. It is concluded that the coagulation defects induced by infusions of high molecular weight dextran are due to intravascular coagulation.

Further Studies on the Effect of Dextran of Various Molecular Weight on the Coagulation Mechanism

1964 ◽  
Vol 11 (01) ◽  
pp. 038-050 ◽  
Author(s):  
Inga Marie Nilsson ◽  
Oddvar Eiken
Keyword(s):  
Molecular Weight ◽  
Body Weight ◽  
Platelet Count ◽  
Bleeding Time ◽  
Average Molecular Weight ◽  
Coagulation Factors ◽  
Factor Vii ◽  
Factor V ◽  
Human Beings ◽  
Coagulation Defect

SummaryDextran fractions of different molecular weights were given to dogs in order to ascertain at which molecular weight dextran interferes with the coagulation factors.1. Infusions of dextran with an average molecular weight of 130,000 (Intradex®) and in doses of 1.5 g dextran per kg body weight induced a moderate coagulation defect. There was a slight prolongation of the bleeding time and a slight drop in platelet count. Values for AHF, factor V, prothrombin and factor VII, and fibrinogen declined by 10 to 40% of the original values.2. Infusions of dextran with an average molecular weight of 75,000 (Macrodex®) in doses of 1.5 g per kg body weight did not produce any significant changes in bleeding time and platelet count. The AHF level decreased by 40% and the levels of prothrombin and factor VII, factor V and fibrinogen by about 10% of the original values. In a dose of 2 g per kg body weight this fraction produced a significant coagulation defect with a fall of the various coagulation factors by about 40 to 50%.3. A dextran fraction with an average molecular weight of 60,000 in doses of 1.5 g per kg body weight did not prolong the bleeding time and caused only a very slight decrease in platelet count. There were no changes in the values for AHF, factor V, prothrombin and factor VII but a slight drop occurred in the fibrinogen levels.4. Dextran with an average molecualr weight of 40,000 (Rheomacrodex ® ) in doses of 1.5 g per kg body weight did not affect the bleeding time or the platelet count. Nor did any significant decline occur in the amounts of the other coagulation factors.No changes in the Duke or in the Ivy bleeding times were observed in human beings given Macrodex® and Rheomacrodex® in doses of 1 g per kg body weight.Intradex® and Macrodex® in doses of up to 1-1.5 g per kg bodyweight to persons with normal blood coagulation are considered not associated with any appreciable risk of haemorrhage, but they are contraindicated in patients with haemorrhagic diathesis. The experiments indicate that Rheomacrodex® in similar doses does not incur any risk of haemorrhage.

FRACTIONATION OF LIVER SOMATOMEDIN ACTIVITY BY ULTRAFILTRATION

1974 ◽  
Vol 62 (2) ◽  
pp. 355-361 ◽  
Author(s):  
JENNIFER M. DEHNEL ◽  
P. D. McCONAGHEY ◽  
M. J. O. FRANCIS
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Weight Fraction ◽  
Low Molecular Weight ◽  
High Molecular Weight Fraction ◽  
Cartilage Growth ◽  
The Relationship ◽  
Somatomedin Inhibitors

SUMMARY Plasma somatomedin is the intermediary through which growth hormone (GH) exerts its effects on the growing skeleton. Somatomedin activity may be produced in vitro by perfusion of the liver and kidneys of rats with Waymouth's medium containing GH. The relationship between the activity of plasma somatomedin and somatomedin of hepatic and renal origin has yet to be clarified. Somatomedin from plasma can be separated into active fractions of both high and low molecular weight. Similarly, ultrafiltration of medium containing somatomedin of hepatic origin indicates the existence of two active fractions, one of high molecular weight (greater than 50000) and one of low molecular weight (less than 1000). The latter can be attributed to the release of amino acids, such as serine and glutamine, by the perfused tissue. The high molecular weight fraction is believed to represent GH-dependent somatomedin. Fractions that inhibit production of cartilage matrix are present in liver perfusates as well as in plasma. These results provide further evidence that the liver is a source of GH-dependent somatomedin in vivo. Furthermore, cartilage growth may be controlled not only by the GH-stimulated release of somatomedin by the liver, but also by its release of acid-labile somatomedin inhibitors.

scholarly journals Deoxyribonucleic acid synthesis in mammalian systems. Permealysed Ehrlich ascites cells in vitro first label Okazaki-type low-molecular-weight deoxyribonucleic acid and then high-molecular-weight deoxyribonucleic acid

1972 ◽  
Vol 130 (4) ◽  
pp. 959-964 ◽  
Author(s):  
Leigh A. Burgoyne
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Deoxyribonucleic Acid ◽  
Acid Synthesis ◽  
Preparation Procedure ◽  
Low Molecular Weight ◽  
Deoxyribonucleic Acid Synthesis ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cells

During the evaluation of a method of preparing permealysed Ehrlich ascites cells, shortterm labelling experiments were carried out with d[3H]TTP. In the first minute the bulk of the label appeared as low-molecular-weight pieces of DNA. Subsequently the label appeared in DNA of much higher molecular weight. A brief description of the preparation procedure and the properties of the product is provided. Evidence is presented to show that the nucleotide was incorporated directly without intermediate conversion into dTMP or thymidine.

Distribution of radioactive silver in the subcellular fractions of various tissues of the rat and its binding to low molecular weight proteins

1983 ◽  
Vol 61 (11) ◽  
pp. 1391-1395 ◽  
Author(s):  
Yousef Matuk
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Filtration ◽  
Total Radioactivity ◽  
Subcellular Fractions ◽  
Low Molecular Weight ◽  
Electron Microscopic ◽  
Molecular Weight Peak

In view of the electron microscopic evidence that silver does not penetrate cellular barriers, the distribution of radioactive silver in rat blood and subcellular fractions of liver, kidneys, spleen, and forebrain was studied. It was found that 24 h after a single intraperitoneal injection high levels of radioactivity were reached which decreased at different rates in the various tissues studied. In plasma, liver, and kidneys there was an initial rapid loss of radioactivity which was followed by a slower rate of loss. In the blood, forebrain, and spleen the loss of radioactivity was linear and somewhat slower than in the other three tissues. The cytosols of the liver and kidneys contained 60% while those of the forebrain and spleen contained 30% of the total radioactivity found in the tissue homogenates. Gel filtration on Sephadex G-75 showed that all cytosols contained two peaks of radioactivity; a high molecular weight peak which eluted just after the void volume and a low molecular weight peak. The amount of radioactivity in both peaks was, however, much lower in the chromatographic peaks of the forebrain and spleen than that found in those of the liver and kidneys. Furthermore, the spleen had a comparatively very small low molecular weight radioactive peak. In vitro experiments with liver cytosol showed similar results to those found in vivo in that the high molecular weight radioactive peak could be removed by heat. It is concluded that silver does enter cells and that silver thionein exists in the cytosols of forebrain, spleen, kidney, and liver.

scholarly journals Low-molecular weight components of cow colostrum regulate bone marrow functions by modelling the redox-system of the organism

2020 ◽  
Vol 11 (2) ◽  
pp. 272-277
Author(s):  
A. I. Bozhkov ◽  
S. L. Ohiienko ◽  
A. Y. Bondar ◽  
E. G. Ivanov ◽  
N. I. Kurguzova
Keyword(s):  
Molecular Weight ◽  
Bone Marrow ◽  
Body Weight ◽  
Large Dose ◽  
Redox System ◽  
Low Molecular Weight ◽  
Lipid Hydroperoxides ◽  
Low Doses ◽  
In Vitro System

Colostrum is rich in various biologically active compounds such as immunotropic ones. Low molecular weight components were isolated from cow colostrum components (with a molecular weight of not more than 45 kDa). Their influence was investigated on intact Wistar Rattus norvegicus adult males in concentrations of 0.01, 0.1, 1.0 and 5.0 g/100 g of body weight. We determined content of lipid hydroperoxides and activity of serum glutathione peroxidase in blood serum, parameters of the bone marrow cells’ (BMCs) behaviour in the in vitro system (proliferation ability, morphologically identifiable and unidentifiable type of cells, lifespan of eosinophils). Morphological identifiable cells were stab neutrophils, segmented neutrophils, metamyelocytes, myelocytes, lymphocytes, basophils, neutrophils, eosinophils, monocytes. The low doses of colostrum components (0.01–0.10 g/100 g of body weight) did not affect the ratio of morphologically identifiable/unidentifiable cells. Administration of colostrum components at low doses (0.01 g/100 g of weight) increased the ability of BMCs to proliferate in the in vitro system. A super-large dose of colostrum components (5 g/100 g of body weight) was accompanied by a further loss of capacity for proliferation and cell death. Moreover, large doses of colostrum components resulted in change of balance to prooxidants (oxidants). The role of redox – system in BMCs functions was discussed. Large doses of colostrum components (1–5 g/100 g of body weight) were accompanied by a change of pro-antioxidant system balance. Only eosinophils were determined after administration of colostrum components in a large dose. It should be noted that the lifetime of eosinophils which developed under influence of colostrum components was greater than that of eosinophils obtained from control animals.

The In Vitro Analysis of the Coagulation Mechanism of Activated Factor VII Using Thrombelastogram

2002 ◽  
Vol 88 (11) ◽  
pp. 768-772 ◽  
Author(s):  
Chiharu Kawaguchi ◽  
Yae Hanesaka ◽  
Akira Yoshioka ◽  
Yukihiro Takahashi
Keyword(s):  
Platelet Rich Plasma ◽  
Coagulation Factor ◽  
Factor Vii ◽  
Factor V ◽  
Coagulation Factor Vii ◽  
Activated Factor Vii ◽  
Coagulation Mechanism ◽  
Vitro Analysis ◽  
Hemostatic Effects

SummaryWe investigated the effects of addition of recombinant activated coagulation factor VII (rFVIIa) to coagulation factor-deficient plasma and whole blood, using thrombelastograms (TEGs). The addition of rFVIIa to factor II-or X-deficient plasma did not correct hemostatic parameters, whereas it produced partial responses in factor V-, VIII-or IX-deficient plasma and good responses in factor VII-, XI-or XII-deficient plasma. Furthermore, the addition of rFVIIa and platelets (30-100 X 103/µl) to platelet-poor plasma produced marked corrections, producing TEGs similar to those of platelet-rich plasma. These results indicate that factors II and X are essential for the hemostatic effects of rFVIIa, and that factors V and VIII promote these effects. We believe that TEGs are, at present, one of the most useful tools for evaluating in vitro hemostatic effects of rFVIIa.

Effects of a Low Molecular Weight Heparin (Fragmin®) and of Unfractionated Heparin on Coagulation Activation at the Site of Plug Formation In Vivo

1994 ◽  
Vol 72 (06) ◽  
pp. 831-835 ◽  
Author(s):  
Sabine Elchinger ◽  
Michael Wolzt ◽  
Malgorzata Nieszpaur-Los ◽  
Barbara Schneider ◽  
Klaus Lechner ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Unfractionated Heparin ◽  
Low Molecular Weight Heparin ◽  
Bleeding Time ◽  
Venous Blood ◽  
Coagulation System ◽  
Low Molecular Weight ◽  
Coagulation Activation

SummaryThe clinical benefits of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) have been shown in many trials. However, the mode of action of heparin has not been fully elucidated. Thus, we wanted to study the effects of UFH and LMWH in vivo by measuring coagulation activation markers in blood obtained directly from a vascular injury site. In a double-blind, randomized, 3-way, cross-over study 18 healthy volunteers were given UFH (150 U/kg s.c.) and 2 doses of LMWH [35 U/kg s.c. (low dose, Id), 75 U/kg s.c. (high dose, hd)]. Prothrombin fragment 1+2 (F1+2), thrombin-antithrombin complex (TAT) and fibrinopeptide A (FPA) were measured in bleeding time blood and in venous blood before and after drug application. In addition, the effects of UFH and LMWH on in vitro coagulation tests were studied. Compared to base line, UFH and both IdLMWH and hdLMWH caused significant reductions of F1+2, TAT and FPA in bleeding time blood at 2 h. A marked effect of UFH and of hdLMWH was also seen at 5 h. The inhibition of FPA generation was more pronounced after hdLMWH compared to IdLMWH. In venous blood, UFH and LMWH caused reductions of F1+2, but not of TAT and FPA. In vitro, UFH predominantly affected the anti-IIa assays (activated partial thromboplastin time, thrombin time) and LMWH mainly the anti-Xa test system. Using a technique that investigates the activated coagulation system in vivo, a time- and dose dependent inhibitory effect of heparin on coagulation activation was detectable. Therefore, in our experimental setting a preferential inhibition of a particular portion of the coagulation system by one of the two heparin preparations was not detectable.

scholarly journals The pupal cuticle of Drosophila: biphasic synthesis of pupal cuticle proteins in vivo and in vitro in response to 20-hydroxyecdysone.

1985 ◽  
Vol 101 (1) ◽  
pp. 189-200 ◽  
Author(s):  
J Doctor ◽  
D Fristrom ◽  
J W Fristrom
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Ultrastructural Changes ◽  
Low Molecular Weight ◽  
Before And After ◽  
Cuticle Protein ◽  
Cuticle Proteins ◽  
Pupal Cuticle

We investigated the synthesis and localization of Drosophila pupal cuticle proteins by immunochemical techniques using both a complex antiserum and monoclonal antibodies. A set of low molecular weight (15,000-25,000) pupal cuticle proteins are synthesized by the imaginal disk epithelium before pupation. After pupation, synthesis of the low molecular weight proteins ceases and a set of unrelated high molecular weight proteins (40,000-82,000) are synthesized and incorporated into the pupal cuticle. Ultrastructural changes in the cuticle deposited before and after pupation correlate with the switch in cuticle protein synthesis. A similar biphasic accumulation of low and high molecular weight pupal cuticle proteins is also seen in imaginal discs cultured in vitro. The low molecular weight pupal cuticle proteins accumulate in response to a pulse of the insect steroid hormone 20-hydroxyecdysone and begin to appear 6 h after the withdrawal of the hormone from the culture medium. The high molecular weight pupal cuticle proteins accumulate later in culture; a second pulse of hormone appears to be necessary for the accumulation of two of these proteins.

On The Conversion Of High Molecular Weight Urokinase To The Low Molecular Weight Form

1981 ◽  
Author(s):  
Grant H Barlow ◽  
Charles W Francis ◽  
Victor J Marder
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Isotonic Saline ◽  
Low Molecular Weight ◽  
Plasmin Activity ◽  
Fibrin Plate ◽  
Gradient Gel Electrophoresis ◽  
Minute Duration

The conversion of high molecular weight urokinase (HMW) to low molecular weight urokinase (LWM) by plasmin in vitro has been studied. The two molecular weight forms of urokinase were separated by SDS polyacrylamide gradient gel electrophoresis and active enzyme extracted from gel segments into isotonic saline after slicing the gel at 5 mm intervals. Extracts from gel segments were analyzed by the fibrin plate method, and electrophoretic separation of the two forms were shown to be complete by comparison with the migration of purified standards and by the absence of lytic zones between the peaks of activity. HMW was incubated with plasminogen and fibrinogen for various time intervals from 2.5 to 10 minutes, enzymatic activity inhibited with aprotinin, and the samples subjected to electrophoresis. Conversion from HMW to LMW was apparent in as little as 2.5 minutes and continued for the 10 minute duration of the experiments. Similar experiments starting with LMW showed no change in molecular weight. Incubation of HMW without plasminogen resulted in no conversion to LMW implying that this reaction was not autocatalytic. The same conversion may occur in vivo during therapeutic administration of urokinase when a “lytic state” is produced and plasmin activity is present. Possible conversion of HMW to LMW in vivo will need to be considered in evaluating the relative therapeutic efficacy of different urokinase preparations and in interpreting the results of clinical trials.

Evaluation of Compounds Extracted from Eight Genera of Wild Mushrooms from Nigeria for Anti-cell Proliferation Activity in Vitro

2019 ◽  
Vol 60 (5) ◽  
pp. 952-960
Author(s):  
Erute Magdalene Adongbede ◽  
Israel Temitope Aduralere
Keyword(s):  
Molecular Weight ◽  
Cell Proliferation ◽  
High Molecular Weight ◽  
Low Molecular Weight ◽  
Wild Mushrooms ◽  
Anti Cancer ◽  
Cell Proliferation Activity ◽  
Low Molecular Weight Compounds ◽  
Proliferation Activity

     Mushrooms have bioactive compounds that have antimicrobial, anti-cancer and antioxidant activities among other medicinal benefits. In the present study, we examined the anti-cell proliferation activities of mushrooms from eight genera obtained from the wild in Nigeria. Saccharomyces cerevisiae was used as a model organism to screen mushroom extracts for anti-cell proliferation activity. Polyphenols, high molecular weight polysaccharides and low molecular weight compounds from aqueous extracts were obtained from the test mushrooms using methanol and water respectively. The extracts were screened in vitro at different concentrations of extracts with the CyQuant cell proliferation assay. The high molecular weight polysaccharides from tested mushrooms reduced cell proliferation (96.79% inhibition in Ganoderma multipileum Ding Hou to 66.71% inhibition in Coltricia perennis (L.) Murrill at 10.00mg/ml). Percentage inhibition caused by low molecular weight compounds varied from 94.22% (Ganoderma multipileum) to 76.19% (Coltricia perennis) at 10mg/ml. Percentage of inhibition with the polyphenols varied from 94.12% (Microporus xanthopus Fr) Kuntze) to 79.82% (Coltricia perennis) at high doses. High molecular polysaccharides, low molecular weight compounds and polyphenols from mushrooms have anti-cancer properties. The CyQUANT assay proliferation kit was a very efficient tool for screening extracts from wild mushrooms for anti-cell proliferation activities. Medicinal mushrooms in Nigeria show a lot of promise as a reservoir for drug discovery particularly in the area of cancer research.

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