Separation of glutathione S-transferase activities with epoxides from the mouse liver h-protein, a major polycyclic hydrocarbon-binding protein

• Published in: Cancer research (Chicago, Ill.) Ill.), 1978-05, Vol.38 (5), p.1438
• Main Authors: Sarrif, A M, McCarthy, K L, Nesnow, S, Heidelberger, C
• Format: Article
• Language: English
• Subjects: 9,10-Dimethyl-1,2-benzanthracene - metabolism; Ammonium Sulfate; Animals; Benz(a)Anthracenes - metabolism; Carboxymethylcellulose Sodium; Chromatography; Epoxy Compounds - metabolism; Glutathione Transferase - immunology; Glutathione Transferase - isolation & purification; Isoelectric Focusing; Liver - metabolism; Mice; Proteins - isolation & purification; Proteins - metabolism
• ISSN: 0008-5472

The C3H mouse liver h-protein is a cytoplasmic protein to which metabolites of carcinogenic polycyclic hydrocarbons bind covalently following i.p. injection. It has a number of physical properties similar to those of the glutathione S-transferases (EC 2.5.1.18). These properties include molecular weight (40,000), number of subunits (2), basic isoelectric point around 8.0, sedimentation coefficient (3.5S), and subcellular localization. In this communication, we have shown that glutathione S-transferase activities with 1,2-epoxy(3-p-nitrophenoxy)propane and benz[a]anthracene 5,6-oxide as substrates were separated from the h-protein on carboxymethylcellulose and isoelectrofocusing columns. The purification of the mouse h-protein as a [3H]-7,12-dimethylbenz[a]anthracene conjugate or as the free form is also described.