By Ciba Foundation
Chapter 1 Chairman's starting comments (pages 1–3): C. Rimington
Chapter 2 The Succinate?Glycine Cycle; The position of ??Aminolevulinic Acid in Porphyrin Synthesis (pages 4–26): David Shemin
Chapter three a few houses 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 sustaining Biosynthesis of other Haemin Chromoproteins, with distinct connection with Cytochrome C; the function of Tissue Organs (pages 96–127): David L. Drabkin
Chapter nine Experimental stories 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 unfastened Erythrocyte Porphyrins to Haemoglobin Biosynthesis (pages 185–195): Leif Eriksen
Chapter 14 experiences of a few Liver Heme Proteins and Porphyrins in Experimental Sedormid Porphyria (pages 196–208): Rudi Schmid and Samuel Sciiwartz
Chapter 15 reviews of Porphyrin Synthesis and Interconversion, with targeted connection with convinced 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 simply by 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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Extra info for Ciba Foundation Symposium - Porphyrin Biosynthesis and Metabolism
Extract acetone-dried ox liver with water Heat for 3 min. at 57" Precipitate with (NH,),SO, between 40 and 55% saturation Adsorb on to Ca,(PO,), gel at pI-1 5 . 6 ; elute at pH 7 - 4 Precipitate with (NH,),SO, between 40 and 55% saturation Adsorb on to Ca,(PO,), gel at pH 5 . 6 ; elute at pH 7 . 4 Precipitate with (NH,),SO, (48% saturation) at pH 5 . 5 -4 X1-3 &AMINOLAEVULIC ACID DEHYDRASE 31 activity is lost in the acetone-drying. The purification procedure, with the approximate purification achieved a t each step, is summarized in Table 111.
2. Absorption spectrum of purified ALAD. no loss of activity between pH 6 . 0. 2. However, changing the dialysis medium does not cause any further loss of activity, although changing the dialysis sac removes a further 30 per cent of the activity. This effect does not seem to be the same as the inactivation of TPN-nitrate reductase described by Nason and Evans (1953). It is hoped to investigate this further. The spectrum of purified ALAD is shown in Fig. 2; 8-AMINOLAEVULIC ACID DEHYDRASE 35 there is no evidence to be obtained from it as t o possible prosthetic groups.
173, 214. LAMPEN, J. , and WANG,T. P. (1952). J. biol. , 198, 385. , and EVANS, H. J. (1953). J . biol. , 202, 655. , and SCOTT,J. J. (1953). , 172,1093. SCHUBERT, M. P. (1937). J . biol. , 121,539. SCOTT,J. J. (1955). Unpublished results. ,and RUSSELL,C. S. (1954). J. Amer. chem. , 76, 1204. , and RUSSELL, C. S. (1953). J. Amer. chem. , 75, 4873. DISCUSSION Gujdos: It is most interesting that Dr. Gibson has found that a great variety of organs are capable of transforming 6-aminolaevulic acid to porphobilinogen in vitro.