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Md Bashir Uddin Byeong-Hoon Lee Chamilani Nikapitiya Jae-Hoon Kim Tae-Hwan Kim Hyun-Cheol Lee Choul Goo Kim Jong-Soo Lee Chul-Joong Kim 《Journal of microbiology (Seoul, Korea)》2016,54(12):853-866
Bee venom (BV) from honey bee (Apis Melifera L.) contains at least 18 pharmacologically active components including melittin (MLT), phospholipase A2 (PLA2), and apamin etc. BV is safe for human treatments dose dependently and proven to possess different healing properties including antibacterial and antiparasitidal properties. Nevertheless, antiviral properties of BV have not well investigated. Hence, we identified the potential antiviral properties of BV and its component against a broad panel of viruses. Co-incubation of non-cytotoxic amounts of BV and MLT, the main component of BV, significantly inhibited the replication of enveloped viruses such as Influenza A virus (PR8), Vesicular Stomatitis Virus (VSV), Respiratory Syncytial Virus (RSV), and Herpes Simplex Virus (HSV). Additionally, BV and MLT also inhibited the replication of non-enveloped viruses such as Enterovirus-71 (EV-71) and Coxsackie Virus (H3). Such antiviral properties were mainly explained by virucidal mechanism. Moreover, MLT protected mice which were challenged with lethal doses of pathogenic influenza A H1N1 viruses. Therefore, these results provides the evidence that BV and MLT could be a potential source as a promising antiviral agent, especially to develop as a broad spectrum antiviral agent. 相似文献
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Mahanama De Zoysa Chamilani Nikapitiya You-Jin Jeon Youngheun Jee Jehee Lee 《Journal of applied phycology》2008,20(1):67-74
A sulfated polysaccharide with anticoagulant properties was isolated from the fermented brown seaweed Sargassum fulvellum. Freeze-dried S. fulvellum was fermented in an incubator for 10th week at 25°C to convert seaweed macromolecules into anticoagulant sulfated polysaccharides (ASP). Anticoagulant activity
was determined by an activated partial thromboplastin time (APTT) test using citrated human blood plasma. The 8th week S. fulvellum crude seaweed extract (SWE) exhibited the highest blood anticoagulant activity. Therefore, 8th week crude SWE was used for purification of ASP by two steps; DEAE cellulose anion-exchange followed by Sepharose 4B chromatography.
The isolated ASP showed a single spot on agarose gel electrophoresis, which confirmed the purification status of our ASP.
Polyacrylamide gel electrophoresis (PAGE) analysis showed that the molecular mass of the purified ASP was between 8 and 20 kDa.
Polysaccharide and sulfate concentrations of the purified ASP were 180 and 29.70 μg mL−1 respectively. ASP recovery was 1.32% (w/w) from the crude polysaccharide applied to the DEAE column. Purified ASP had a pH
of 3.86 and was considered an acidic polysaccharide. Moreover, both ASP and heparin showed a relative clotting factor of 27.47
at the concentrations of 180 and 60 μg mL−1 respectively. Therefore, S. fulvellum ASP can be considered a weaker anticoagulant than heparin. Results of the APTT, PT, and TT clotting assays showed that ASP
was able to inhibit both intrinsic and extrinsic blood coagulation pathways. Finally, this study established a feasible and
simple experimental protocol to isolate anticoagulant from fermented seaweeds leading to potential further development of
anticoagulant agent for the pharmaceutical industry. 相似文献
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Chulhong Oh Chamilani Nikapitiya Youngdeuk Lee Ilson Whang Se-Jae Kim Do-Hyung Kang Jehee Lee 《Journal of industrial microbiology & biotechnology》2010,37(5):483-494
A gene (agrP) encoding a β-agarase from Pseudoalteromonas sp. AG4 was cloned and expressed in Escherichia coli. The agrP primary structure consists of an 870-bp open reading frame (ORF) encoding 290 amino acids (aa). The predicted molecular
mass and isoelectric point were determined at 33 kDa and 5.9, respectively. The signal peptide was predicted to be 21 aa.
The deduced aa sequence showed 98.6% identity to β-agarase from Pseudoalteromonas atlantica. The recombinant protein was purified as a fusion protein and biochemically characterized. The purified β-agarase (AgaP)
had specific activity of 204.4 and 207.5 units/mg towards agar and agarose, respectively. The enzyme showed maximum activity
at 55°C and pH 5.5. It was stable at pH 4.5 to 8.0 and below 55°C for 1 h. The enzyme produced neoagarohexaose and neoagarotetraose
from agar and in addition to that neoagarobiose from the agarose. The neoagarooligosaccharides were biologically active. Hence,
AgaP is a useful enzyme source for use by cosmetic and pharmaceutical industries. 相似文献