Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme fromLachesis muta rhombeataSnake Venom

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis muta rhombeata Snake Venom

We report a rapid purification method using one-step chromatography of SVSP Rhombeobin (LMR-47) from Lachesis muta rhombeata venom and its procoagulant activities and effects on platelet aggregation. The venom was fractionated by a single chromatographic step in RP-HPLC on a C8 Discovery BIO Wide Pore, showing high degree of molecular homogeneity with molecular mass of 47035.49 Da. Rhombeobin s...

متن کامل

Purification and Partial Characterization of a Thrombin-Like Enzyme (AH144) from Venom of Iranian Snake Agkistrodon Halys

The snake venom´s thrombin-like enzymes comprise a number of serine proteases, which are functionally and structurally related to thrombin. Purification and partial characterization of a thrombin-like enzyme from the venom of the Iranian snake, Agkistrodon halys, was the aim of this study. Purification was carried out by a combination of variety of chromatographic methods that included: gel...

متن کامل

purification and partial characterization of a thrombin-like enzyme (ah144) from venom of iranian snake agkistrodon halys

the snake venom´s thrombin-like enzymes comprise a number of serine proteases, which are functionally and structurally related to thrombin. purification and partial characterization of a thrombin-like enzyme from the venom of the iranian snake, agkistrodon halys, was the aim of this study. purification was carried out by a combination of variety of chromatographic methods that included: gel fil...

متن کامل

Thrombin - like Enzyme from the Venom of Bitis gubonicu

Gabonase, an enzyme which acts on fibrinogen and factor XI11 in uniquely thrombin-like ways, was purified to electrophoretic homogeneity from the venom of Bitis gabonica. On sodium dodecyl sulfate-polyacrylamide electrophoresis, the reduced protein behaved as a single chain with Mr = 30,600. The enzyme contains 20.6% carbohydrate, no free sulfhydryl groups and hence, from amino acid analysis, f...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: BioMed Research International

سال: 2013

ISSN: 2314-6133,2314-6141

DOI: 10.1155/2013/903292