Anomalous reaction of 4-chloro-7-nitrobenzofurazan with thiol compounds

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

Impairment of the catalytic activity of Escherichia coli ribonucleic acid polymerase by a unique reaction of 4-chloro-7-nitrobenzofurazan.

Escherichia coli RNA polymerase loses 55-65% of its catalytic activity on reaction with Nbf-Cl (4-choro-7-nitrobenzofurazan). This partial inactivation was shown to be the result of specific impairment of RNA-chain elongation, since initiation of RNA chains was not altered after treatment with Nbf-Cl. The site of reaction was shown to be a unique thiol on the beta-subunit. This thiol is not acc...

متن کامل

Synthesis of 4-aryloxy-7-nitrobenzofurazan Derivatives from 4-chloro-7-nitrobenzofurazan and Various Phenoxide Anions (Including Pharmaceuticals) in the Presence of Crown Ethers

4-Chloro-7-nitrobenzofurazan reacts by nucleophilic substitution with phenoxide anions derived from estriol (2c), ethynylestradiol (2d), phenol (3e), guaiacol (3f ), 2,6dimethoxyphenol (3g), eugenol (3h), isoeugenol (3i), the cytostatic Etoposide (4), and Reichardt’s betaine (5) in the presence of crown ethers a¬ording the corresponding 4-aryloxy7-nitrobenzofurazan derivatives 6c, 6d, 7e { 7i, ...

متن کامل

A method for determining the adenosine triphosphatase content of energy-transducing membranes. reaction of 4-chloro-7-nitrobenzofurazan with the adenosine triphosphatase of bovine heart submitochondrial particles.

1. Modification of a single amino acid residue by introduction of the nitrobenzofurazan group inactivates mitochondrial ATPase (adenosine triphosphatase) when membrane-bound in submitochondrial particles. The similarity between the reactions of both membrane-bound and isolated ATPase with 4-chloro-7-nitrobenzofurazan indicates that the single essential tryosine residue identified in the isolate...

متن کامل

Reaction of Thiol Compounds with Peroxidase and Hydrogen Peroxide*

Recent studies have indicated that peroxidase might function in the biological synthesis of thyroxine by the thyroid gland. Johnson and Tewkesbury (1) believed that thyroxine might be formed by the oxidative coupling of 2 molecules of diiodotyrosine. Westerfeld and Lowe (2) studied the oxidative condensation of p-cresol by hydrogen peroxide and peroxidase and suggested that peroxidase might be ...

متن کامل

Reaction of thiol compounds with peroxidase and hydrogen peroxide.

Recent studies have indicated that peroxidase might function in the biological synthesis of thyroxine by the thyroid gland. Johnson and Tewkesbury (1) believed that thyroxine might be formed by the oxidative coupling of 2 molecules of diiodotyrosine. Westerfeld and Lowe (2) studied the oxidative condensation of p-cresol by hydrogen peroxide and peroxidase and suggested that peroxidase might be ...

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: Biochemical Journal

سال: 1979

ISSN: 0264-6021

DOI: 10.1042/bj1770385