Glutathione transferase of human breast is closely related to transferase of human placenta and erythrocytes.
An acidic form (pI 4.6) of glutathione transferase has been purified to homogeneity from normal and tumor specimens of human breast. The two proteins did not differ significantly in their molecular and catalytic properties. The enzyme has a molecular weight of 46,000 and is composed of two identical subunits. The data presented, including amino acid composition, substrate specificity and immunological studies, give strong evidence that the glutathione transferase of human breast, placenta and erythrocytes are similar if not identical proteins.
D000596:Amino Acids / Q000032:analysis; D001940:Breast / Q000201:enzymology*; D001943:Breast Neoplasms / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D005982:Glutathione Transferase / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009928:Organ Specificity; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D013379:Substrate Specificity
D000596:Amino Acids; D005982:Glutathione Transferase