By P. M. Harrison, E. R. Bauminger, D. Hechel, N. W. Hodson, I. Nowik, A. Treffry (auth.), Chaim Hershko, Abraham M. Konijn, Philip Aisen (eds.)
The 4th foreign convention on Hemochromatosis and the eleventh foreign convention on Iron and Iron Proteins came about in Jerusalem on April 27 -30 and on may perhaps 2 -7 1993, respectively. the 1st, a scientific assembly, and the second one, a discussion board designed essentially for uncomplicated scientists. either conferences are held on a regular basis on regulate nate years and signify essentially the most vital discussion board for the trade of knowledge in iron study. the current quantity "Progress in Iron study" relies on a variety of displays brought at those conferences. even though, this quantity represents even more than a booklet of convention complaints. It deals a accomplished state of the art overview on so much elements of iron metabolism. we have now attempted to provide a balanced evaluation of crucial fresh advancements in iron study together with either uncomplicated learn and medical research. in spite of the fact that, the scope of chapters used to be established, by means of definition, at the genuine individuals on the conferences and a few vital fields in iron learn similar to plant body structure, microbial facets of iron metabolism, and loose radical learn haven't been handled. a number of the authors of the forty chapters have beel). pt1rsonally accountable for probably the most very important advancements in iron learn ~~vidffig: n~~~ights into iron body structure and pathophysiology. The Editors desire to convey their gratitude for the exceptional and well timed cooperation of all members to this volume.
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Public Health Service. REFERENCES 1. H. K. L. Simmons, and D. W. lnvest. 38:161 (1959). 2. -y'Y. Hu and P. Strud. 8:349 (1978). 3. A. B. H. Biol. Chern. 254:9943 (1979). 4. S. B. Sci. A. 78:3039 (1981). 5. M. K. H. Biochem. 92:147 (1978). 6. e. Kiihn, A. H. Ruddle, Gene transfer, expression and molecular cloning of the human transferrin receptor gene, Cell 37:95 (1984). 7. B. S. Chern. 256:4715 (1981). 8. -I. Do, e. D. Chern. 265:114 (1990). 9. A. M. L. I. -I. Do, and e. BioL Chern. 266: 13272 (1991).
I- 100 100 80 80 Q) 0 0 '0 0---_9 60 ::I 0 CD Q) ---0----0""9,,,,_ 40 • • L... _ c "'~ 40 • 20 0 8 • 20 Q) 0... 0 0 2 4 6 Time (min) 8 10 0 0 2 4 6 8 10 Time (min) Fig. 3. 6. A, C-tenninal monoferric transferrin; B, N-tenninal monoferric transferrin. Data from Ref. 28. Receptor-Induced Switch in Site-Site Cooperativity during Iron Release Interactions between the sites of transferrin in their strengths of iron-binding an in the facility with which they relinquish specifically bound metal ions to iron chelators have previously been reported30•31 • As has often been observed with other multisited proteins, occupancy of one site influences the binding properties of its partner site(s), presumably as a result of long-range conformational changes.
1988, Mechanism of iron uptake: Activity of the H-chain and deletion mapping of the ferroxidase site. A study of iron uptake and ferroxidase activity of human liver, recombinant H-chain ferritins and of two H-chain deletion mutants, J. Bioi. Chem. 263:18086. 10. , Levi, S. and Chasteen, N. , 1993, Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin and site-directed mutants, submitted for publication. 11. , Domer, M. , 1989, Expression and structural and functional properties of human L ferritin from Escherichia coli, Biochemistry 28:5179.