Properties of glutathione insulin transhydrogenase from beef liver.

نویسنده

  • H H TOMIZAWA
چکیده

The glutathione-insulin transhydrogenase from beef liver haa been found to promote the reductive cleavage of the disulfide bonds of insulin by simple sulfhydryl compounds such as glutathione (2). The properties of this enzyme are of interest not only because of its probable involvement in the biological regulation of the level of insulin but also because, at present, it is the only isolated mammalian enzyme that can catalyze the reductive cleavage of a protein. The present paper describes some of the properties of the beef liver glutathione-insulin transhydrogenase.

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Glutathione-insulin Transhydrogenase of Human Liver.

An enzyme which promotes the degradation of insulin has been isolated from beef liver (2, 3). This enzyme, which has been designated glutathione-insulin transhydrogenase (4), catalyzes the reductive cleavage of the disulfide bonds of insulin by a simple sulfhydryl compound such as glut,athione (4, 5). Because the process of degradation may be important in the etiology of diabetes mellitus, expe...

متن کامل

Assay of Microsomal Membrane-bound Glutathione-insulin Transhydrogenase and Comparison with Protein

1. Inhibition of endogenous microsomal NADPH oxidase by CO enables membranebound glutathione-insulin transhydrogenase (EC 1.8.4.2) to be assayed conveniently by a linked assay involving NADPH and glutathione reductase (EC 1.6.4.2). 2. The specific activity of the enzyme in rat liver microsomal preparations is of the order of 1 nmol of oxidized glutathione formed/min per mg of membrane protein. ...

متن کامل

Studies on the Specificity and Mechanism of Action of Hepatic Glutathione - Insulin

Studies on the specificity and mechanism of action of hepatic glutathione-insulin transhydrogenase, an enzyme capable of catalyzing the reductive cleavage of the disulfide bonds of insulin in the presence of excess reduced glutathione, have been carried out. By coupling reactions catalyzed by glutathione-insulin transhydrogenase to that of glutathione reductase, it was indicated that during the...

متن کامل

Studies on the specificity and mechanism of action of hepatic glutathione-insulin transhydrogenase.

Studies on the specificity and mechanism of action of hepatic glutathione-insulin transhydrogenase, an enzyme capable of catalyzing the reductive cleavage of the disulfide bonds of insulin in the presence of excess reduced glutathione, have been carried out. By coupling reactions catalyzed by glutathione-insulin transhydrogenase to that of glutathione reductase, it was indicated that during the...

متن کامل

Resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography.

1. Protein disulphide-isomerase (EC 5.3.4.1) and glutathione-insulin transhydrogenase (EC 1.8.4.2) were resolved by covalent chromatography. Both activities, in a partially purified preparation from bovine liver, bind covalently as mixed disulphides to activated thiopropyl-Sepharose 6B, in a new stepwise elution procedure protein disulphide-isomerase is displaced in mildly reducing conditions w...

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

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 237  شماره 

صفحات  -

تاریخ انتشار 1962