Renin: Purification, structure determination and active site.

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

Purification of acetylcholinesterase by affinity chromatography and determination of active site stoichiometry.

Specific inhibitors of acetylcholinesterase have been prepared and attached to Sepharose. When crude preparations of the enzyme are chromatographed on the aflinity gel, the enzyme is selectively retained and may be eluted by a salt gradient. Conditions have been defined under which enzyme is purified some ZO-fold in one step to a homogeneous and apparently pure species. An essential factor appe...

متن کامل

Two-site direct immunoassay specific for active renin.

A sensitive immunoradiometric assay, without an enzymatic step and specific for active human renin, was developed with use of two monoclonal antibodies (MAbs). In this assay system, the first MAb was coupled to magnetic beads (Magnogel); the second one, directed against the active form of the enzyme, was radiolabeled with 125I. The specificity of this assay was demonstrated in experiments measu...

متن کامل

Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen.

In order to carry out studies on structure and function relationships of porcine pepsinogen using site-directed mutagenesis approaches, the cDNA of this zymogen was cloned, sequenced, expressed in Escherichia coli, and the protein refolded, and purified to homogeneity. Porcine pepsinogen cDNA, obtained from a lambda gt10 cDNA library of porcine stomach contains 1364 base pairs. It contains lead...

متن کامل

Purification of renin and prorenin.

In this issue of the journal, we feature two articles—one by Tadashi Inagami and the other by Pierre Corvol and Joel Menard—relating the story of the purification of renin. These investigators received the 1985 CIBA Award for Hypertension Research for biochemical studies leading to the isolation, amino acid structural and three-dimensional configuration, and the physiochemical and immunochemica...

متن کامل

Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination.

D-Amino acid aminotransferase was found in several thermophilic Bacillus species and purified to homogeneity from the best producer, Bacillus sp. YM-1, which was newly isolated from a sauna dust. The enzyme has a molecular weight of about 62,000 and consists of two subunits identical in molecular weight (30,000). It catalyzes transamination between various D-amino acids and alpha-keto acids, al...

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 Japan Academy, Series B

سال: 1986

ISSN: 0386-2208,1349-2896

DOI: 10.2183/pjab.62.197