Redox forms of human placenta glutathione transferase.

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

Redox forms of human placenta glutathione transferase.

Human placenta glutathione transferase (EC 2.5.1.18) pi undergoes an oxidative inactivation which leads to the formation of an inactive enzymatic form which is homogeneous in several chromatographic and electrophoretic conditions. This process is pH dependent, and it occurs at appreciable rate in alkaline conditions and in the presence of metal ions. Dithiothreitol treatment completely restores...

متن کامل

Glutathione Transferase from Bovine Placenta

A method was developed to purify glutathione transferase from bovine placenta by affinity chromatography and fast protein liquid chromatography. The purified enzyme was homogeneous as judged by sodium dodecyl sulfate gel electrophoresis and isoelectric focusing. The dimeric enzyme is composed of identical subunits with a molecular weight of 23,000; its isoelectric point is 6.9. In contrast to p...

متن کامل

Expression of cytochrome P450 and glutathione S-transferase in human bone marrow mesenchymal stem cells

Currently several studies are being carried out on various properties of mesenchymal stem cells (MSCs)however there are a few investigations about drug metabolizing properties of these cells. The aim of thisstudy was to measure the key factors involved in drug metabolism in human bone marrow MSCs. For thispurpose, cellular glutathione (GSH), glutathione Stransferase (GSTs) and...

متن کامل

Erythrocyte glutathione S-transferase. Electrophoretic identification of two enzyme forms.

Starch-gel electrophoresis was used to demonstrate two forms of glutathione S-transferase in human erythrocytes. Whereas considerable inter-individual differences in enzyme activity and electrophoretic patterns were detected, intra-individual differences were small.

متن کامل

Human glutathione S-transferases. Characterization of the anionic forms from lung and placenta.

Anionic glutathione S-transferases were purified from human lung and placenta. Chemical and immunochemical characterization, including polyacrylamide-gel electrophoresis, gave strong evidence that the anionic lung and placental enzymes are chemically similar, if not identical, proteins. The electrophoretic mobilities of both proteins were identical in conventional alkaline gels as well as in ge...

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: Journal of Biological Chemistry

سال: 1991

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)54653-6