کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1978356 | 1061539 | 2007 | 10 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A new lectin from the sea worm Serpula vermicularis: Isolation, characterization and anti-HIV activity A new lectin from the sea worm Serpula vermicularis: Isolation, characterization and anti-HIV activity](/preview/png/1978356.png)
A GlcNAc-specific lectin was isolated from the sea worm Serpula vermicularis (SVL) (Annelida) and purified by ion-exchange, affinity and gel permeation chromatography. SVL was a homotetrameric protein with native molecular mass of about 50 kDa, and consisted of identical subunits of 12.7 kDa. The carbohydrate content of 1.9% suggested that the lectin was a glycoprotein, and mainly composed by aspartic and glutamic acids, glycine, valine and serine; with relatively lower content of basic amino acids and cysteine. The first 15 residues of the N-terminal region were determined as ADTPCQMLGSRYGWR. It was stable at pH 6–9 and at temperatures up to 40 °C. SVL was Ca2+-independent lectin that agglutinated native and trypsinized human erythrocytes. Hapten inhibition studies indicated that SVL showed binding specificity only for N-acetyl-d-glucosamine and its derivatives among the monosaccharides tested and required the presence of hydroxyl group at the C-3 of GlcNAc. The presence of hydrophobic p-nitrophenyl aglycone improved inhibitory potency of N-acetyl-d-glucosamine. Ovomucoid and ovalbumin were found to be inhibitors among the glycoproteins used for inhibition assay. The anti-HIV-1 (human immunodeficiency virus) activity of SVL in vitro was determined: SVL inhibited the production of viral p24 antigen and cytopathic effect induced by HIV-1. The EC50 values were 0.23 and 0.15 μg·mL− 1 respectively.
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 145, Issue 2, March 2007, Pages 184–193