کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8395783 | 1544142 | 2015 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of two platelet-aggregation inhibitors, named angustatin and H-toxin TA2, from the venom of Dendroaspis angusticeps
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
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چکیده انگلیسی
Angustatin and H-toxin TA2 were purified from unfractionated Dendroaspis angusticeps venom (0.3 g) using S-Sepharose fast flow column chromatography, gelfiltration on a Sephadex G-50 column, and reverse-phase HPLC. The purified materials strongly inhibited ADP-induced platelet aggregation. The primary structure of angustatin was determined by the Edman degradation of peptides derived from digestions with endopeptidese Arg-C and α-chymotrypsin. Angustatin, which was composed of 59 amino acid residues and an RGD sequence, was identified as a short-length inhibitor similar to mambin, dendroaspin, echistatin, and eristicophin. Angustatin shared 83%, 17%, and 15% homologies with mambin, eristicophin, and echistatin, respectively. On the other hand, H-toxin TA2 did not conserve the RGD sequence in its structure; it was replaced for the Glu-Met-Leu sequence. Furthermore, the amino acid sequence of H-toxin TA2 corresponded to toxin TA2, excluding the amino acid residue of His28Arg.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 93, January 2015, Pages 61-67
Journal: Toxicon - Volume 93, January 2015, Pages 61-67
نویسندگان
Etsuko Oyama, Hidenobu Takahashi,