By G. Schapira (auth.), F. Gross (eds.)

ISBN-10: 3642871526

ISBN-13: 9783642871528

ISBN-10: 3642871542

ISBN-13: 9783642871542

International Symposia subsidized through ClBA Basle were held every year considering 1959 in a number of eu international locations. In con­ trast to the various clinical conferences organised by way of the ClBA FOUN­ DATION both at its headquarters in London or sometimes in a foreign country, the themes handled at those overseas Symposia have con­ cerned difficulties extra at once concerning ClBA'S personal examine paintings within the pharmaceutical box. a number of the issues coated as much as the current replicate the far-reaching pursuits and the large­ unfold actions pharmaceutical firm develops in relatively diversified fields of chemical, organic, and scientific study, and to which the ba.sic method is an more and more vital prerequisite for the improvement of a brand new and worthy healing agent. Iron metabolism got here into the sector of curiosity in reference to CIBA'S learn on antibiotics and similar average items containing iron, components which act of their metal-free shape as powerful and particular chelating brokers. after all, those observations, attention-grabbing notwithstanding they're, wouldn't in themselves have justi­ fied a symposium. It appeared, notwithstanding, valuable to check the hot effects from a much broader point of view and to try to narrate them to present-day wisdom of iron metabolism ordinarily its body structure, its pathology, and healing elements. The luck of a systematic symposium is dependent upon the concep­ tion of the programme and the choice of the participants.

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EHRENBERG, and B. CHANCE: Arch. Biochem. ) 37, 237 (1952). - 21. URRY, D. , and H. EYRING: Proc. Nat. Acad. Sc. A. 49, 253 (1963). - 22. VALENTINE, R. , R. L. JACKSON, and R. S. WOLFE: Biochem. Biophys. Res. Comm. ) 7, 453 (1962). 23. WHATLEY, F. , K. TAGAWA, and D. I. ARNON: Proc. Nat. Acad. Sc. A. 49, 266 (1963). - 24. WILLIAMS, R. J. : Chem. Rev. i6, 299 (1955). Discussion LONDON: Dr. EICHHORN, you made the important point that the electronic configuration of the iron helps to determine the biological function of the various haem proteins.

RITTENBERG: I have often thought that the function of the various complexes of iron in the organism is to keep the iron in solution. At pH 7, Fe+++ is quite insoluble. The function of the porphyrin complexes is to combine with four sites of the octahedral configuration of iron. The four sites lie in one plane and prevent the other two sites lying on each side of the plane from being complexed by a simple amino acid. I wonder whether the importance of the protein in a metallic protein lies in its contribution not only to specificity but also to solubilisation of the metal.

Thus, we have the feeling that the in vitro inhibition by lead is artificial and may be explained by the protein-precipitating effect of lead. Now, in lead-poisoned animals, haem synthesis is actually diminished. We think that one of the reasons for this is the enhancing effect of lead on iron accumulation in the stroma of the red cells. This was shown by JANDL 2 , and we could entirely confirm his findings. YOSHIKAWA: I don't know whether lead acts as a real inhibitor of enzyme activity or whether it just denaturates the enzyme protein.

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Iron Metabolism: An International Symposium by G. Schapira (auth.), F. Gross (eds.)

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