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By Ciba Foundation

ISBN-10: 0470718943

ISBN-13: 9780470718940

ISBN-10: 0470722371

ISBN-13: 9780470722374

Chapter 1 Chairman's establishing comments (pages 1–3): C. Rimington
Chapter 2 The Succinate?Glycine Cycle; The function of ??Aminolevulinic Acid in Porphyrin Synthesis (pages 4–26): David Shemin
Chapter three a few homes of ??Aminolaevulic Acid Dehydrase (pages 27–42): ok. D. Gibson
Chapter four The Metabolism of ??Aminolaevulic Acid (pages 43–62): J. J. Scott
Chapter five Haem and Porphyrin Formation from Porphobilinogen Glycine, ??Aminolaevulic Acid and Porphobilinogen (pages 63–71): J. E. Falk
Chapter 6 The function of a few Porphyrins and Porphyrin Precursors within the Biosynthesis of Haem (pages 72–85): Elisabeth I. B. Dresel
Chapter 7 at the Synthes is and Metabolism of C14?Labelled Hematoporphyrin (pages 86–95): Kurt I. Altman, A. okay. Bruce and ok. Salomon
Chapter eight self reliant Biosynthesis of alternative Haemin Chromoproteins, with certain connection with Cytochrome C; the position of Tissue Organs (pages 96–127): David L. Drabkin
Chapter nine Experimental reviews of Porphyrin Metabolism in Cytochrome C Synthesis (pages 128–142): A. Vannotti
Chapter 10 Porphyrin and Chlorophyll Biosynthesis in Chlorella (pages 143–155): S. Granick
Chapter eleven Heterogeneous Metabolism of Haemoglobins (pages 156–173): G. Schapira, J?C. Dreyfus and J. Kruh
Chapter 12 mobile Formation of Intermediates in the course of Haemoglobin Synthesis (pages 174–184): Bo Thorell
Chapter thirteen Relation of loose Erythrocyte Porphyrins to Haemoglobin Biosynthesis (pages 185–195): Leif Eriksen
Chapter 14 reviews of a few Liver Heme Proteins and Porphyrins in Experimental Sedormid Porphyria (pages 196–208): Rudi Schmid and Samuel Sciiwartz
Chapter 15 experiences of Porphyrin Synthesis and Interconversion, with exact connection with yes eco-friendly Porphyrins in Animals with Experimental Hepatic Porphyria (pages 209–228): Samuel Schwartz and Kojun Ikeda
Chapter sixteen Metabolism of Porphobilinogen and of Porphyrins within the Rabbit (pages 229–245): Alfred Gajdos and Marianne Gajdos?Torok
Chapter 17 Precursors of Porphyrin and Porphobilinogen (pages 246–253): P. Formijne and 9 J. Poulie
Chapter 18 reviews at the Mechanism of Porphyrin Biosynthesis through Inhibitors (pages 254–264): W. Stich and P. Decker
Chapter 19 The Formation of Porphyrins by means of Photosynthetic micro organism (pages 265–284): June Lascelles
Chapter 20 The Synthesis of the Uroporphyrins II and IV (pages 285–302): S. F. MacDonald and Karl?Heinz Michl

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172,292. FOSTER, G. , and SHEMIN, D. (1955). Unpublished findings. , and SHEMIN, D. (1955). Unpublished findings. GIBSON,K. , and SCOTT, J. J. (1954). Biochem. , 58,xli. , (1954). Science, 120,1105. ,KAMEN, M. , andMooRE, C. V. (1948). J. biol. , 174,767. KARLSSON, J. , and BARKER, H. A. (1949). J. biol. , 177,597. , and SHEMIN, D. Unpublished results. LONDON, I. M. and YAMASAKI, M. (1952). Fed. , 11, 250. , and NEUBERGER, A. (1949). Biochem. , 45, 163. , and NEUBERGER, A. (1950). Biochern. , 47,97.

Evidence has been obtained that ALAD is a sulphydryl enzyme. 1. Activation of ALAD by GSH and CSH, at pH 6 . 8 and 38", 0 4 GSH; 0-0, CSH is necessary to add cysteine (CSH) or glutathione (GSH) in order t o obtain any activity. Ascorbic acid and sodium dithionite are without effect. BAL is an effective activator, but thioglycollic acid does not activate. The effect of increasing the concentration of GSH and CSH is shown in Fig. 1 ; from these curves it appears that GSH is a more effective activator than CSH.

Evidence for the existence of such an enzyme was first obtained by Dresel and Falk (1953), and it was presumably present in the soluble porphyrinforming enzyme system described by Shemin, Abramsky and Russell (1954). In this communication some studies of the distribution and properties of ALAD will be described; a preliminary note has appeared already (Gibson, Neuberger and Scott, 1954). Granick (1954) has independently reported some work on the ALAD ofrchicken erythrocytes. Estimation It has been found that if the reaction is carried out in vacuo PBG is not metabolized further even in the presence of crude preparations of ALAD.

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