scholarly journals The effect of fiber and mortar type on the freezing and thawing resistance of Slurry Infiltrated Fiber Concrete (SIFCON)

Author(s):  
A A Manolia ◽  
A S Shakir ◽  
J F Qais
2014 ◽  
Vol 584-586 ◽  
pp. 1304-1308 ◽  
Author(s):  
Sheng Ji Jin ◽  
Zhong Liang Li ◽  
Jian Zhang ◽  
Yan Ling Wang

The concrete composite material with basalt fiber as enhancing system in it has a lot of advantages ,including excellent mechanical properties , high temperature resistant, resistant to acid and alkali, low cost, environmental protection materials and resistance production process. It has been applied to the field of construction project. Damage of northern environment of freezing and thawing on the properties of the composite material has become a new hot issue. In order to study the characteristics of basalt fiber reinforced concrete as building composite materials in the process of freezing and thawing, this research uses the freeze-thaw cycle test to carry out the performance study on change of dynamic modulus of elasticity and quality loss of basalt fiber concrete. We use basalt fiber volume content of 0, 0.1%, 0.2% and 0.3% respectively of four groups of concrete specimens as the research object, to carry them on the freezing-thawing resisting performance test research. Research results show that the performance of dynamic modulus of elasticity and quality loss of basalt fiber concrete in freezing and thawing process is obviously better than the plain concrete. The dosage of 0.3% basalt fiber concrete freezing-thawing resisting performance is the best in the four groups of concrete samples.


Author(s):  
José L. Carrascosa ◽  
José M. Valpuesta ◽  
Hisao Fujisawa

The head to tail connector of bacteriophages plays a fundamental role in the assembly of viral heads and DNA packaging. In spite of the absence of sequence homology, the structure of connectors from different viruses (T4, Ø29, T3, P22, etc) share common morphological features, that are most clearly revealed in their three-dimensional structure. We have studied the three-dimensional reconstruction of the connector protein from phage T3 (gp 8) from tilted view of two dimensional crystals obtained from this protein after cloning and purification.DNA sequences including gene 8 from phage T3 were cloned, into Bam Hl-Eco Rl sites down stream of lambda promotor PL, in the expression vector pNT45 under the control of cI857. E R204 (pNT89) cells were incubated at 42°C for 2h, harvested and resuspended in 20 mM Tris HC1 (pH 7.4), 7mM 2 mercaptoethanol, ImM EDTA. The cells were lysed by freezing and thawing in the presence of lysozyme (lmg/ml) and ligthly sonicated. The low speed supernatant was precipitated by ammonium sulfate (60% saturated) and dissolved in the original buffer to be subjected to gel nitration through Sepharose 6B, followed by phosphocellulose colum (Pll) and DEAE cellulose colum (DE52). Purified gp8 appeared at 0.3M NaCl and formed crystals when its concentration increased above 1.5 mg/ml.


1978 ◽  
Vol 40 (02) ◽  
pp. 288-301 ◽  
Author(s):  
P Meucci ◽  
I R Peake ◽  
A L Bloom

SummaryFactor VIII-related activities have been studied in platelet fractions in order to try to reconcile the conflicting findings of other workers, and to extend the studies. In platelets from 16 normal subjects procoagulant factor VIII was not detected. The amount of factor VIII-related antigen (FVIIIR: AG) in the cytosol per mg of protein was about twice that in the membrane fraction and about ten times that in the debris fraction. There was no significant difference between the amount of FVIIIR: AG and ristocetin cofactor (RistCof) activity in each fraction. The findings in haemophilic platelets were similar. In von Willebrand’s disease (vWd) one serverely affected patient had no detectable factor VIII related activities in any platelet fraction. In 5 patients with intermediate vWd results were normal. In a further 5, with more prolonged bleeding times, no FVIIIR: RistCof was detected in platelets, despite a normal amount of FVIIIR: AG in the cytosol and debris. The electrophoretic mobility of cytosol FVIIIR: AG was increased in all normals and patients, while that in the membrane and debris fractions had normal mobility. Cytosol FVIIIR: AG eluted later than normal FVIIIR: AG on gel filtration on Sepharose 2B, and also showed reduced antibody binding in an immunoradiometric assay. Precipitation of FVIIIR: AG by concanavalin A was incomplete in all platelet fractions from normals, and even more reduced in vWd platelet fractions. The results suggest the possibility of two types of platelet FVIIIR: AG.A factor VIII-related antigen was shown to be associated with normal washed platelets by immunofluorescence techniques (Bloom et al. 1973). Since then, several studies have been reported on the localisation of factor VIII related antigen (FVIIIR: AG), factor VIII procoagulant activity (FVIII: C) and factor VIII related ristocetin cofactor activity (FVIIIR: RistCof) within the platelets. Initially, Howard et al. (1974) indicated that FVIIIR: AG was firmly bound to the platelet membrane, and noted that in lysed platelets the level of FVIIIR: AG as measured by electroimmunodiffusion was higher than that in whole platelet suspensions. However, further studies by Nachman and Jaffe (1975) showed that FVIIIR: AG was also present to a considerable extent in the granules, and they detected none in the platelet cytosol. Bouma and colleagues (1975) were, however, able to find FVIIIR: AG and FVIIIR: RistCof in the cytosol upon freezing and thawing platelets. This FVIIIR: AG had an electrophoretic mobility comparable to that of normal plasma. They also noted that platelets which were air dried apparently had a granular FVIIIR:AG localisation by immunfluorescence; however, intact platelets in suspension did not stain by this method.Recently Ruggeri et al. (1977) and Sultan et al. (1977) have also found FVIIIR: AG in the cytosol, and the former authors reported it to have increased electrophoretic mobility when compared to normal plasma FVIIIR:AG. Results concerning the localisation of FVIIIR: AG in normal platelets have thus been conflicting. Similarly, in the few reports available concerning platelet FVIIIR: AG in von Willibrand’s disease variable results have also been obtained (Ruggeri et al. 1977, Howard et al. 1974, Shearn et al. 1974 and Bouma et al. 1975).In this study we report on the localisation of factor VIII-related activities in normal, haemophilic and von Willebrand’s disease platelets using available standard techniques as well as precipitation of FVIIIR: AG with the plant lectin concanavalin A, a procedure which has been shown to detect abnormal forms of FVIIIR:AG in certain types of von Willebrand’s disease (Peake and Bloom 1977).


1981 ◽  
Vol 45 (01) ◽  
pp. 038-042 ◽  
Author(s):  
M E Pogliani ◽  
R Fantasia ◽  
G Lambertenghi-Deliliers ◽  
E Cofrancesco

SummaryThe influence of Daunorubicin on some platelet functions in vitro was investigated, using different concentrations of the drug (0.01-0.02-0.04 μg/ml). Daunorubicin was shown to inhibit Collagen and Thrombin induced platelet aggregation and the intensity of inhibition depended on both drug concentration and the time of preincubation.Daunorubicin was also shown to inhibit the release reaction, the platelet prostaglandin pathway and the availability platelet factor 3; the drug at concentrations for clinical use does not damage the platelet membrane, as is the case with the freezing and thawing test, in platelet uptake of 14C-serotonin and as confirmed by the electron microscope. When very high doses (0.16 mg) of Daunorubicin are used, lysis of the platelets can be observed and this is confirmed under the electron microscope by the presence of empty platelets with fractures at the level of the cytoplasmic membrane.Finally, Daunorubicin causes irreversible inhibition of reptilase clot-retraction, even if this is less severe than with Vincristine. Working with gel-filtered platelets, it would appear that the inhibition exercised by the drug on platelet reactions is not caused through modifications in Ca++ metabolism.The authors suggest that Daunorubicin, at the dosages used clinically, induces in vitro thrombocytopathy without damaging the cellular membrane as confirmed by the electron microscope.This impairment of platelet functions could play a part in hemorrhagic diathesis observed during Daunorubicin therapy.


1970 ◽  
Vol 23 (02) ◽  
pp. 261-275 ◽  
Author(s):  
G Zbinden ◽  
J. N Mehrishi ◽  
S Tomlin

SummaryThe severity of platelet damage induced by hyper- and hypotonic NaCl solutions and freezing and thawing was assessed by microscopic evaluation and measuring inhibition of 5-HT uptake. The same techniques were used to quantitate the effects of aggregating agents. The positively charged macromolecules PS, Poly-L und Poly-O reduced the net negative surface charge as determined by microelectrophoresis, caused platelet aggregation and inhibited 5-HT uptake. The damaging effects of Poly-L and Poly-O were more severe and more closely related to concentration than that of PS. The negatively charged macromolecules Poly-IC and NaPS increased the anodic electrophoretic mobility. Poly-IC and heparin caused a low degree of platelet clumping and no inhibition of 5-HT uptake. NaPS produced severe platelet damage with extensive clumping and complete inhibition of 5-HT uptake. Na laurate had the same effect, but did not alter electrophoretic mobility. ADP caused concentration-dependent platelet aggregation and inhibition of 5-HT uptake. The effects of ADP and NaPS were compared in agitated and non-agitated platelet samples containing identical concentrations of the 2 compounds. Agitation was found to increase the degree of platelet clumping and to reduce 5-HT uptake.


1969 ◽  
Vol 21 (03) ◽  
pp. 419-427 ◽  
Author(s):  
N. O Solum ◽  
S Łopaciuk

Summary1. Platelet fibrinogen has been purified from washed bovine platelets. The procedure was based on the methods for purification of plasma fibrinogen by fractionated precipitations and extractions with ethanol and glycine below 0°, and precipitation of proteins by dimethylformamide at 0°.2. The platelet extract obtained by freezing and thawing of the cells, freed from insoluble material by centrifugation at 23,000 x g for 30 min, contained 0.22 ±0.003mg fibrinogen per 109 platelets. Total protein of this fraction was 0.77 ±0.08 mg per 109 platelets whereas that of the insoluble fraction was 0.79 ±0.09 mg per 109 platelets.3. The most purified platelet fibrinogen fraction contained 91-98% of the protein in a thrombin-clottable state. The yield was approx. 20%. It showed homogeneity in analytical ultracentrifugation, in immunoelectrophoresis using an antiserum produced by immunization of rabbits against platelet extract, and in starch gel electrophoresis using a discontinuous system of Tris HCl and borate buffers offering a high resolution power towards the platelet proteins. Polyacrylamide disc electrophoresis revealed two to three faint lines behind the main fibrinogen line. At least one such line was also observed with purified plasma fibrinogen.


1985 ◽  
Vol 54 (03) ◽  
pp. 599-602 ◽  
Author(s):  
M Léon Alhenc-Gelas ◽  
M Aiach ◽  
A Gorenflot ◽  
J P Andreux

SummaryImmunoreactive AT III was found in human platelets. AT III antigen was quantified in platelets taken from each of 17 healthy donors by a specific competitive enzyme immunoassay using purified AT III and AT III antibodies. AT III antigen levels in extracts of washed platelets disrupted by freezing and thawing ranged from 32 to 140 ng per 109 platelets with a mean value of 70.3 ± 27.3. When stimulated by arachidonic acid, the platelets released AT III antigen together with immunoreactive fibrinogen. These results show that AT III is present in platelets at a level corresponding to approximately 0.01% of total antithrombin in normal blood, and suggest that platelet AT III, like fibrinogen, is contained in the storage granules.


1966 ◽  
Vol 53 (2) ◽  
pp. 271-285 ◽  
Author(s):  
Claude Simon ◽  
Marie Roques ◽  
Janine Torresani ◽  
Serge Lissitzky

ABSTRACT The effect of propylthiouracil on the maturation of rat thyroglobulin in vivo has been investigated. Newly iodinated thyroglobulin dimer is labile to freezing and thawing. This observation has been used to interpret the findings in the present experiments. From experiments using rats in isotopic equilibrium with 125I, and treated with propylthiouracil or propylthiouracil and tri-iodothyronine and also given a single injection of 131I, the following conclusions were formulated 1) the appearance of iodinated S12 thyroglobulin monomer is due to the dissociation of labile iodinated thyroglobulin dimer and appears more readily if the dimer is poorly iodinated, 2) uniodinated thyroglobulin dimer is the most probable substrate for iodination in vivo, 3) maturation of thyroglobulin dimer (as shown by increasing sedimentation constant from 16—17 to 19) is accompanied by increasing amounts of iodine in the molecule, 4) it is not possible to say at present if iodination and iodothyronine formation is the cause or the consequence of thyroglobulin dimer maturation, 5) propylthiouracil might inhibit thyroglobulin maturation by decreasing iodine organification.


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