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  1. Jaganathan SK, Mani MP
    3 Biotech, 2018 Aug;8(8):327.
    PMID: 30073112 DOI: 10.1007/s13205-018-1356-2
    In this study, a wound dressing based on polyurethane (PU) blended with copper sulphate nanofibers was developed using an electrospinning technique. The prepared PU and PU nanocomposites showed smooth fibers without any bead defects. The prepared nanocomposites showed smaller fiber (663 ± 156.30 nm) and pore (888 ± 70.93 nm) diameter compared to the pristine PU (fiber diameter 1159 ± 147.48 nm and pore diameter 1087 ± 62.51 nm). The interaction of PU with copper sulphate was evident in the infrared spectrum through hydrogen-bond formation. Thermal analysis displayed enhanced weight residue at higher temperature suggesting interaction of PU with copper sulphate. The contact angle measurements revealed the hydrophilic nature of the prepared nanocomposites (71° ± 2.309°) compared with pure PU (100° ± 0.5774°). The addition of copper sulphate into the PU matrix increased the surface roughness, as revealed in the atomic force microscopy (AFM) analysis. Mechanical testing demonstrated the enhanced tensile strength behavior of the fabricated nanocomposites (18.58 MPa) compared with the pristine PU (7.12 MPa). The coagulation assays indicated the enhanced blood compatibility of the developed nanocomposites [activated partial thromboplastin time (APTT)-179 ± 3.606 s and partial thromboplastin time (PT)-105 ± 2.646 s] by showing a prolonged blood clotting time compared with the pristine PU (APTT-147.7 ± 3.512 s and PT-84.67 ± 2.517 s). Furthermore, the hemolysis and cytotoxicity studies suggested a less toxicity nature of prepared nanocomposites by displaying low hemolytic index and enhanced cell viability rates compared with the PU membrane. It was observed that the fabricated novel wound dressing possesses better physicochemical and enhanced blood compatibility properties, and may be utilized for wound-healing applications.
    Matched MeSH terms: Whole Blood Coagulation Time
  2. Tan NH, Fung SY, Yap YH
    PMID: 21983189 DOI: 10.1016/j.cbpb.2011.09.009
    A thrombin-like enzyme (termed albolabrase) was isolated in purified form from the venom of Cryptelytrops albolabris (white-lipped tree viper) using high performance anion ion exchange and gel filtration chromatography. The molecular mass of albolabrase was 33.7 kDa as determined by SDS-PAGE and 35.8 kDa as determined by Superose gel filtration chromatography. The N-terminal sequence was determined to be VVGGDECNINE which is homologous to many snake venom thrombin-like enzymes. Albolabrase exhibits both arginine ester hydrolase and arginine amidase activities and the enzyme is fastidious towards tripeptide chromogenic anilide substrates. The fibrinogen clotting activity was optimum at 3mg/mL bovine fibrinogen, and showed distinct species differences in the following decreasing order: bovine fibrinogen>dog fibrinogen≈human fibrinogen>goat fibrinogen. The enzyme failed to clot both rabbit and cat fibrinogens. Reversed-phase HPLC analysis on the breakdown products of fibrinogenolytic action of albolabrase indicated that the enzyme belongs to the AB class of snake venom thrombin-like enzyme. In the indirect ELISA, IgG anti-albolabrase reacted extensively with most crotalid venoms, except with Tropidolaemus wagleri and Calloselasma rhodostoma venoms. The double sandwich ELISA, however, showed that anti-albolabrase reacted strongly only with venoms from the Trimeresurus complex, and that the results support the proposed new taxonomy changes concerning the Trimeresurus complex.
    Matched MeSH terms: Whole Blood Coagulation Time
  3. Tan NH, Tan CS
    Toxicon, 1989;27(3):349-57.
    PMID: 2543103
    Trimeresurus wagleri (speckled pit viper) venom exhibited the usual set of enzyme activities occurring in pit viper venoms but the content of alkaline phosphomonoesterase was unusually high, whereas the proportions of protease and arginine ester hydrolase were very low. The venom also exhibited weak thrombin-like activity but did not exhibit hemorrhagic or anticoagulant activity. Analysis of the Sephadex G-200 gel filtration fractions of the venom indicated that the lethal fraction was a low mol.wt protein, and that fractions exhibiting phosphodiesterase, phosphomonoesterase, arginine ester hydrolase, thrombin-like enzyme, L-amino acid oxidase and phospholipase A activities were not lethal. Two lethal toxins, designated as wagleri toxins 1 and 2, were isolated from the venom using Sephadex G-50 gel filtration chromatography followed by SP-Sephadex C-25 ion exchange chromatography. The mol.wts of the two toxins were 8900 by gel filtration. The LD50 (i.v.) values in mice for wagleri toxins 1 and 2 are 0.17 microgram/g and 0.19 microgram/g, respectively.
    Matched MeSH terms: Whole Blood Coagulation Time
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