A cloning strategy to obtain recombinant proteins with identical primary structure to the native forms.
نویسندگان
چکیده
Recombinant gene strategies using fusion tags for purification are essential procedures to obtain large protein quantities. However, most cloning systems result in recombinant proteins with added amino acids inexistent in their native forms which can lead to significant changes in protein properties. An original and simple cloning strategy is proposed to obtain proteins identical in amino acid sequence to the native proteins.
منابع مشابه
A novel chimeric recombinant protein PDHB-P80 of Mycoplasma agalactiae as a potential diagnostic tool
The aim of this study was to construct, expression of a novel recombinant chimeric protein consisting of Pyruvate dehydrogenase beta subunit (PDHB) and high antigenic region of integral membrane lipoprotein P80 of Mycoplasma agalactiae as a potential diagnostic tool. The full-length sequence of pdhb and a portion of antigenic regions of P80 were selected and analyzed by CLC ma...
متن کاملCloning and Sequence Analysis of Gene Encoding OipA from Iranian Clinical Helicobacter pylori
Background: Outer inflammatory protein A (OipA) is one of the important adhesins of H. pylori and a valuable candidate for vaccine development. Its gene is under "on-off" switch status which correlates with OipA protein expression. Objectives: We aimed to obtain a recombinant OipA clone (with "on" status) from an Iranian clinical isolate. Materials and Methods: A clinical H. pylori-isolate demo...
متن کاملCloning, Expression, and Purification of a GDSL-like Lipase/Acylhydrolase from a Native Lipase-Producing Bacterium, Lactobacillus fermentum
Background: Lipase enzymes are of great importance in various industries. Currently, extensive efforts have been focused on exploring new lipase producer microorganism as well as genetic and protein engineering of available lipases to improve their functional features. Methods: For screening lipase-producing lactobacilli, isolated strains were inoculated onto tributyrin agar plates. Molecular ...
متن کاملA Convenient Method for Solubilization and Refolding Recombinant Proteins: An Experience from Recombinant Mouse TGF-β1
Background: The production of recombinant proteins in Escherichia coli is one of the most valuable achievements in biotechnology, with many therapeutic and diagnostic applications; however, the aggregation and misfolding of proteins that result in the formation of insoluble inclusion bodies is a disruptive factor in this process. Various solubilization and refolding methods can be used to impro...
متن کاملDesign, cloning, expression and evaluation of cysteine-substitutes of intact and truncated molecules of streptokinase
Introduction: Thrombosis and the blockage of blood vessels with clots, can lead to acute myocardial infarction and some times even death. Aside from surgical interventions to remove the blockage, the only available treatment is the administration of thrombolytic agents to dissolve the blood clot. Streptokinase (SK) is the most commonly used fibrinolytic drug for this purpose. However, SK...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of biotechnology
دوره 149 1-2 شماره
صفحات -
تاریخ انتشار 2010