کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2065188 | 1076910 | 2009 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification, characterization, and cDNA cloning of acidic platelet aggregation inhibiting phospholipases A2 from the snake venom of Vipera lebetina (Levantine viper)
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کلمات کلیدی
TFAUPLCLysoPCp-BPBVipera lebetina - lebetina افعیphospholipase A2 - آنزیم فسفولیپاز A2 Trifluoroacetic acid - اسید TrifluoroaceticSnake venom - زهر مارLysophosphatidylcholine - لیزوفسفاتیدیل کولینmatrix assisted laser desorption ionization time-of-flight mass spectrometry - ماتریس با استفاده از طیف سنجی جرمی یونیزاسیون یونیزاسیون لیزر جذب می شودMALDI-TOF MS - مالدی توف MSPlatelet aggregation inhibition - مهار تجمع پلاکتultra performance liquid chromatography - کروماتوگرافی مایع با عملکرد فوق العادهcDNA cloning - کلونینگ cDNA
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Purification, characterization, and cDNA cloning of acidic platelet aggregation inhibiting phospholipases A2 from the snake venom of Vipera lebetina (Levantine viper) Purification, characterization, and cDNA cloning of acidic platelet aggregation inhibiting phospholipases A2 from the snake venom of Vipera lebetina (Levantine viper)](/preview/png/2065188.png)
چکیده انگلیسی
Two novel acidic phospholipase A2s (PLA2) were isolated by size exclusion chromatography and reversed-phase chromatography from the crude Vipera lebetina venom. The molecular masses of VLPLA2-1 (13,704Â Da) and VLPLA2-2 (13,683Â Da) and their internal tryptic peptides were determined by MALDI-TOF mass-spectrometry. When tested in human platelet-rich plasma, both enzymes showed a potent inhibitory effect on aggregation induced by ADP and collagen. Chemical modification with p-bromophenacylbromide abolished the enzymatic activity of PLA2; its anti-platelet activity was fully inhibited in case of collagen as inducer and partially inhibited in case of ADP as inducer. The complete cDNAs encoding PLA2 were cloned from a single venom gland cDNA library. Complete amino acid sequences of the VLPLA2 were deduced from the cDNA sequences. The full-length cDNA sequences of the VLPLA2 possess 615Â bp and encode an open reading frame of 138 amino acids that include signal peptide (16 amino acids) and mature enzyme (122 amino acids). The VLPLA2s have significant sequence similarity to many other phospholipase A2s from snake venoms. The phylogenetic analysis on the basis of the amino acid sequence homology demonstrates that VLPLA2s grouped with other Asp49 PLA2s and they appear to share a close evolutionary relationship with the European vipers.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 54, Issue 4, 15 September 2009, Pages 429-439
Journal: Toxicon - Volume 54, Issue 4, 15 September 2009, Pages 429-439
نویسندگان
Heiki Vija, Mari Samel, Ene Siigur, Anu Aaspõllu, Katrin Trummal, Külli Tõnismägi, Juhan Subbi, Jüri Siigur,