کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10803833 | 1057185 | 2013 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom: Molecular sequence analysis of its cDNA and biochemical properties
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کلمات کلیدی
PNAPMSFAnimal venomsTLCKSBTIDeglycosylationα-N-benzoyl-DL-arginine-p-nitroanilideFpA - FPAp-Nitroanilide - p-nitroanilideThrombin-like enzyme - آنزیم مانند ترومبینTame - تامPhenylmethanesulfonyl fluoride - فنیل متیل سولفونیل فلورایدfibrinopeptide A - فیبرینوپپتید AFibrinogen - فیبرینوژنsoybean trypsin inhibitor - مهارکننده تریپسین سویا
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom: Molecular sequence analysis of its cDNA and biochemical properties Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom: Molecular sequence analysis of its cDNA and biochemical properties](/preview/png/10803833.png)
چکیده انگلیسی
The thrombin-like enzyme from Bothrops barnetti named barnettobin was purified. We report some biochemical features of barnettobin including the complete amino acid sequence that was deduced from the cDNA. Snake venom serine proteases affect several steps of human hemostasis ranging from the blood coagulation cascade to platelet function. Barnettobin is a monomeric glycoprotein of 52Â kDa as shown by reducing SDS-PAGE, and contains approx. 52% carbohydrate by mass which could be removed by N-glycosidase. The complete amino acid sequence was deduced from the cDNA sequence. Its sequence contains a single chain of 233 amino acid including three N-glycosylation sites. The sequence exhibits significant homology with those of mammalian serine proteases e.g. thrombin and with homologous TLEs. Its specific coagulant activity was 251.7Â NIH thrombin units/mg, releasing fibrinopeptide A from human fibrinogen and showed defibrinogenating effect in mouse. Both coagulant and amidolytic activities were inhibited by PMSF. N-deglycosylation impaired its temperature and pH stability. Its cDNA sequence with 750Â bp encodes a protein of 233 residues. Indications that carbohydrate moieties may play a role in the interaction with substrates are presented. Barnettobin is a new defibrinogenating agent which may provide an opportunity for the development of new types of anti-thrombotic drugs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 95, Issue 7, July 2013, Pages 1476-1486
Journal: Biochimie - Volume 95, Issue 7, July 2013, Pages 1476-1486
نویسندگان
Dan E. Vivas-Ruiz, Gustavo A. Sandoval, Julio Mendoza, Rosalina R. Inga, Silea Gontijo, Michael Richardson, Johannes A. Eble, Armando Yarleque, Eladio F. Sanchez,