2002
DOI: 10.1006/fsim.2001.0392
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1,3-β-D glucan binding protein (BGBP) from the white shrimp, Penaeus vannamei, is also a heparin binding protein

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Cited by 12 publications
(9 citation statements)
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“…In previous work, HDL-BGBP was purified by heparin affinity chromatography [15], however by this combined method we obtained good yields of HDL-BGBP and the buoyant density was 1.19 g/ml as reported before. Purified HDL-BGBP was observed as a band of ~ 100 kDa detected by SDS-PAGE, Fig.…”
Section: Hdl-bgbp Purificationsupporting
confidence: 59%
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“…In previous work, HDL-BGBP was purified by heparin affinity chromatography [15], however by this combined method we obtained good yields of HDL-BGBP and the buoyant density was 1.19 g/ml as reported before. Purified HDL-BGBP was observed as a band of ~ 100 kDa detected by SDS-PAGE, Fig.…”
Section: Hdl-bgbp Purificationsupporting
confidence: 59%
“…Plasma was centrifuged at 1,000 x g to remove blood cells (hemocytes) and precipitated by dialysis against distilled water as previously described [15]. The pellet was resuspended in buffer 50 mM Tris-HCl (pH 7.5) and subjected to density gradient ultracentrifugation in a similar procedure as previously described [16].…”
Section: Hdl-bgbp Purificationmentioning
confidence: 99%
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“…Surprisingly, no lectin-coding gene was identified in C. gigas libraries but one gene, beta-1,3-glucan binding protein, was identified. This protein is thought to play an important role in the innate immune response of crustaceans and insects because binding of lipopolysaccharide and beta-1,3-glucan binding protein activates the prophenoloxidase (proPO) cascade (Jimenez-Vega et al, 2002). This beta-1,3-glucan binding protein gene is also known to be up-regulated by bacterial and fungal infections in shrimp and the protein produced could be an inducible acute-phase protein that may play a critical role in host-parasite interactions (Roux et al, 2002).…”
Section: Discussionmentioning
confidence: 99%
“…βGBP from M. rosenbergii serum was purified by affinity chromatography on heparin column following the method of Jimenez‐Vega, Sotelo‐Mundo, Ascencio and Vargas‐Albores () with minor modifications. In brief, 2 mL of HEPARIN HYPER D sorbent (PALL Life Sciences, Port Washington, NY, USA) was packed in a small glass column (C1708, Genei, Bengaluru, India) and equilibrated with Tris citrate buffer (0.05 M Tris citrate with 0.15 M NaCl, pH 7.4).…”
Section: Methodsmentioning
confidence: 99%