ENDONUCLEASE II OF E. coli, I. ISOLATION AND PURIFICATION

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود 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

Isolation and purification of CeqI endonuclease, an isoschizomer of EcoRV.

Ooryrprvcterium equii produces a new restriction endonuclease, an iso-schizemer of EcoKV (1). The bacterial strain does not contain significant levels of other nucleases, so the restriction endonuclease activity can be detected in crude extracts. Ihe enzyme is purified by ammonium sulphate fractionation (50-70 % saturation) and DEAE cellulose chranatography (elutes with 200 mM KC1 in PC buffer)...

متن کامل

Purification, biochemical characterization and protein-DNA interactions of the I-CreI endonuclease produced in Escherichia coli.

I- CreI is a member of the LAGLI-DADG family of homing nucleases; however, unlike most members of this family it contains only a single copy of this signature motif. I- CreI was over-expressed in Escherichia coli, and a simple purification protocol developed that gave reasonably pure protein in high yield. Size-exclusion chromatography and chemical cross-linking indicated that the protein is a ...

متن کامل

Mutants of Escherichia coli lacking endonuclease I, ribonuclease I, or ribonuclease II.

To isolate mutants of Escherichia coli K-12 lacking endonuclease I activity (end), a method has been developed which detects, by differential methyl green staining, undegraded deoxyribonucleic acid (DNA) in colonies previously incubated in toluene. This procedure allows isolation of mutant strains in which DNA degradation is reduced. For half of these strains, this defect has been correlated wi...

متن کامل

Synthesis and Production of Sweet-Tasting Protein in E. coli and Purification by Amylose Resin

A sweet water-soluble protein that reminds stable over wide ranges of temperature and pH, Brazzein has various applications. Its tastes like cane sugar but have no calories. However, the extraction of brazzein from its natural source is expensive and not applicable. In this study we used recombinant DNA technology to provide an alternative option for cheaper mass production of brazzein. A brazz...

متن کامل

Cloning, Expression and Purification of Creatininase From Pseudomonas Pseudoalkaligene KF707 in E. coli.

Creatinine amidohydrolase(EC 3.5.2.10) catalyzes the reversible conversion of creatinine to creatine. Creatininase in combination with other enzymes is used for detection of creatinine in serum and urine which is of significant value for detection of renal, muscular and thyroid functions. The aim of this study was to produce recombinant creatininase enzyme in E.coli expression system to use it ...

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: Proceedings of the National Academy of Sciences

سال: 1969

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.62.3.934