The subunit composition and assembly mechanisms of ferritin from various sources will be examined. Aspects of primary structure, conformation and molecular interactions will be probed by physical and chemical means, in an effort to gain insight into the mechanisms by which the protein mediates iron deposition and mobilization in mammalian cells. Aspects of microheterogeneity of different ferritins will be related to subunit heterogeneity. The two classes of subunits found in most ferritins (H and L types) will be purified to homogeneity, and reassembled to form discrete apoferritin moieties. Iron loading functions, and other properties of these apoferritins will be studied. Specific antisera (H or L) will be prepared to determine levels of different species of ferritin in tissues and sera. Biosynthesis studies and mechanisms of differential regulation of the two subunits in response to iron will be investigated in detail.
| Homma, H; Maruyama, H; Niitsu, Y et al. (1986) A subclass of glutathione S-transferases as intracellular high-capacity and high-affinity steroid-binding proteins. Biochem J 235:763-8 |
| Niitsu, Y; Adachi, C; Takahashi, F et al. (1985) Concentration-dependent sedimentation properties of ferritin: implications for estimation of iron contents of serum ferritins. Am J Hematol 18:363-71 |
| Homma, H; Listowsky, I (1985) Identification of Yb-glutathione-S-transferase as a major rat liver protein labeled with dexamethasone 21-methanesulfonate. Proc Natl Acad Sci U S A 82:7165-9 |
| Homma, H; Listowsky, I (1985) Temperature dependent redistribution among the multiple forms of rat Yb-glutathione-S-transferase. Biochem Biophys Res Commun 127:425-32 |
