Porphyrin biosynthesis in Euglena gracilis-VI. The effect of growth conditions on porphobilinogenase activity and further properties

1. 1. The effect of light and growing time on chlorophyll, protein content and the activity of porphobilinogenase (PBGase), in Euglena gracilis was studied. 2. 2. It was found that neither protein nor chlorophyll content or PBGase activity were dependent upon the days of growing or the light conditi...

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Autor principal: Rossetti, M.V
Otros Autores: Araujo, L.S, Lombardo, M.E, García, S.C, del C. Batlle, A.M
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1987
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100 1 |a Rossetti, M.V. 
245 1 0 |a Porphyrin biosynthesis in Euglena gracilis-VI. The effect of growth conditions on porphobilinogenase activity and further properties 
260 |c 1987 
270 1 0 |m del C. Batlle, A.M.; Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), (CONICET-Facultad de Ciencias Exactas y Naturales, UBA) Ciudad Universitaria, Pabellón II 20 Piso, 1428 Buenos Aires Argentine, Argentina 
506 |2 openaire  |e Política editorial 
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504 |a Batlle, del, Tigier, Llambias, Wider, Biosintesis de porfirinas en callos de soya—XIV. Cambios en la actividad de la delta-amino dehidrasa con las condiciones de crecimiento (1975) Anal. Asoc. Quim. Arg., 63, pp. 305-312 
504 |a Baltersby, Baldas, Collins, Gayson, James, McDonald, Mechanism of biosynthesis of the vynil groups of protoporphyrin IX (1972) J. chem. Soc. chem. Commun., 1265-1266 
504 |a Battersby, Buckley, McDonald, Williams, Enzymic formation of the type III porphyrin macrocycle from unrearranged APAP pyrromethane (1977) Journal of the Chemical Society, Chemical Communications, pp. 115-117 
504 |a Battersby, Fookes, Gustafson-Potter, Matcham, McDonald, Proof by synthesis that unrearranged hydroxymethylbilane is the product from deaminase and the substrate for cosynthetase in the biosynthesis of Urogen III (1979) Journal of the Chemical Society, Chemical Communications, pp. 1155-1158 
504 |a Battersby, Fookes, Gustafson-Potter, McDonald, Matcham, Biosynthesis of porphyrins and related macrocycles. Part 171.2. Chemical and enzymic transformation of isomeric aminomethylbilanes into uroporphyrinogens: proof that unrearranged bilane is the preferred enzymic substrate and detection of a transient intermediate (1982) Journal of the Chemical Society, Perkin Transactions 1, 1, pp. 2413-2426 
504 |a Battersby, Fookes, Gustafson-Potter, McDonald, Matcham, Biosynthesis of porphyrins and related macrocycles. Part 181.2. Proof by spectroscopy and synthesis that unrearranged hidroxymethylbilane is the product from deaminase and the substrate for cosynthelase in the biosynthesis of uroporphyrinogen III (1982) Journal of the Chemical Society, Perkin Transactions 1, 1, pp. 2427-2444 
504 |a Battersby, Fookes, Matcham, McDonald, Hollenstein, Biosynthesis of porphyrins and related macrocycles Part 20 Purification of deaminase and studies on its mode of action (1983) Journal of the Chemical Society, Perkin Transactions 1, 1, pp. 3031-3040 
504 |a Battersby, Fookes, Matcham, Pandey, Biosynthesis of porphyrins and related macrocycles Part 21 The interaction of deaminase and its products (hydroxyethylbilane) and the relationship between deaminase and cosynthetase (1983) Journal of the Chemical Society, Perkin Transactions 1, 1, pp. 3041-3047 
504 |a Battersby, Fookes, McDonald, Meegan, Biosynthesis of type III porphyrins (1978) Proof of intact enzymic conversion of the head-to-tail bilane into Urogen III by intramolecular rearrangement, pp. 185-186. , J. Am. chem. Soc 
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504 |a Battersby, Hunt, McDonald, Biosynthesis of type III porphyrins (1973) Nature of the rearrangement process, pp. 442-443. , J. chem Soc. chem. Commun 
504 |a Battersby, Johnson, McDonald, Williams, Mechanistic study of the enzymic incorporation of unrearranged APAP pyrromethane into Urogen III (1977) Journal of the Chemical Society, Chemical Communications, pp. 117-119 
504 |a Battersby, McDonald, Williams, Wurziger, Biosynthesis of the natural (type III) porphyrins (1977) Proof that rearrangement occurs after head-to-tail bilane formation, pp. 113-115. , J. chem. Soc. chem. Commun 
504 |a Bogorad, Jacobson, Inhibition of greening of etiolated leaves by actinomycin D (1964) Biochem. Biophys. Res. Commun., 14, pp. 113-117 
504 |a Carell, Kahn, Synthesis of porphyrins by isolated chloroplasts of Euglena (1964) Archs Biochem. Biophys., 108, pp. 1-6 
504 |a Carell, Price, Porphyrins and the iron requirement for chlorophyll formation in Euglena (1965) Plant. Physiol., 40, pp. 1-7 
504 |a Cavaleiro, Kenner, Smith, Biosynthetic intermediates between coproporphyrinogen III and protoporphyrin IX (1973) Journal of the Chemical Society, Chemical Communications, pp. 183-183 
504 |a Clement, Kohashi, Piper, Rat liver purification uroporphyrinogen III-cosynthetase (1982) Archs Biochem. Biophys., 214, pp. 657-661 
504 |a Conford, Transformation of PBG into porphyrins by preparations from human erythrocytes (1964) Biochem. J., 91, pp. 64-73 
504 |a Dubash, Rege, Excretion of protoporphyrin IX by Euglena (1967) Biochim. biophys. Acta, 141, pp. 209-211 
504 |a Ebbon, Tait, Studies on S-adenosyl-methionine-magnesium protoporphyrin methyltransferase on Euglena gracilis strain Z (1969) Biochem. J., 3, pp. 573-582 
504 |a Fumagalli, Kotler, Rossetti, Batlle, Human red cell porphobilinogen deaminase (1985) A simpler method of purification and some unusual properties, 17, pp. 485-494. , Int. J. Biochem 
504 |a Fumagalli, Rossetti, Juknat, Kotler, Batlle, Estudios sobre la PBG-asa de higado de cerdo (1982) Anal. Assoc. Quim. Arg., 70, pp. 375-382 
504 |a Gassman, Bogorad, Control of chlorophyll production in rapidly greening bean leaves (1967) PLANT PHYSIOLOGY, 42, pp. 774-780 
504 |a Gassman, Bogorad, Studies on the regeneration of protochlorophyllide after brief illumination of etiolated bean leaves (1967) PLANT PHYSIOLOGY, 42, pp. 781-784 
504 |a Granick, Magnesium protoporphyrin mono-ester and proroporphyrin monomethyl ester in chlorophyll biosynthesis (1961) J. biol. Chem., 236, pp. 1168-1172 
504 |a Granick, (1963) Cytodifferential and Macromolecular Synthesis, p. 144. , M. Locke, Academic Press, New York 
504 |a Hart, Battersby, Purification and properties of uroporphyrinogen III synthease (cosynthetase) from Euglena gracilis (1985) Biochem. J., 232, pp. 151-160 
504 |a Hart, Leeper, Battersby, Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5′-phosphate (1984) Biochem. J., 222, pp. 93-102 
504 |a Hovenkamp-Obbema, Effect of added aminolaevulinic acid upon synthesis of chlorophyll in Euglena gracilis (1975) Zeitschrift für Pflanzenphysiologie, 75, pp. 1-5 
504 |a Juknat, Biosintesis enzimática de porfirinógenos (1983) Doctoral thesis, , University of Buenos Aires, Argentine 
504 |a Juknat, Rossetti, Batlle, Porphyrin biosynthesis in Euglena gracilis IV (1981) An endogenous factor controlling the enzymic synthesis of porphyrinogens and its possible role in the treatment of some porphyrias, 13, pp. 343-353. , Int. J. Biochem 
504 |a Kirk, Studies on the dependence of chlorophyll synthesis on protein synthesis in Euglena gracilis, together with a nomogram for determination of chlorophyll concentration (1968) Planta, 78, pp. 200-207 
504 |a Kirk, Allen, Dependence of chloroplast pigment synthesis on protein synthesis: effect of actidiona (1965) Biochim. Biophys. Res. Commun., 21, pp. 523-530 
504 |a Kotler, Fumagalli, Juknat, Batlle, Porphyrin biosynthesis in Rhodopseudomonas palustris—IX (1986) Deaminase: Kinetics studies, , Int. J. Biochem., in press 
504 |a Llambias, Batlle, Porphyrin biosynthesis in soybean callus-V (1970) The porphobilinogen deaminase-uroporphyrinogen III cosynthetase system Kinetics studies, 220, pp. 552-559. , Biochim. biophys. Acta 
504 |a Llambias, Batlle, Negative homotropic kinetics of soybean callus porphobilinogen deaminase-uroporphyrinogen III cosynthetase (1970) FEBS Lett., 9, pp. 180-182 
504 |a Llambias, Batlle, Studies on the porphobilinogen deaminase-uroporhyrinogen cosynthetase system of culture soybean cells (1971) Biochem J, 121, pp. 327-340 
504 |a Llambias, Batlle, Porphyrin biosynthesis-VII (1971) Biochim Biophys Acta, 227, pp. 180-191. , Biochim. biophys. Acta 
504 |a Llambias, Locascio, Batlle, Porphyrin biosynthesis-IX (1971) Porphobilinogen deaminase-uroporphyrinogen III cosynthetase from avian erythrocytes, 59, pp. 271-278. , Anal. Assoc. Quim. Arg 
504 |a Lockwood, Rimington, Purification of an enzyme converting porphobilinogen to uroporphyrinogen (1957) Biochem. J., 67, pp. 8-13 
504 |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275 
504 |a Marguiles, Effect of chloramphenicol on formation of chloroplast structure and protein during greening of etiolated leaves of Phaseolus vulgaris (1966) PLANT PHYSIOLOGY, 41, pp. 992-1003 
504 |a Moore, Labbe, Assays for ALA and PBG determination (1964) Clin. Chem., 10, pp. 1105-1109 
504 |a Price, Vallee, Euglena gracilis a test organism for study of zinc (1962) PLANT PHYSIOLOGY, 37, pp. 428-433 
504 |a Richard, Nigon, La production d'acide δ-aminolévulinique au cours du verdissement d'euglénes etiolées et ses relations avec la photosynthése (1972) C.r. Acad. Sci. Paris, 274-500, pp. 1307-1310 
504 |a Richard, Nigon, La synthése de lácide δ-aminolévulinique et de la chlorophylle lors de léclairement d' Euglena gracilis etiolées (1973) Biochim. biophys. Acta, 313, pp. 130-149 
504 |a Rimington, Spectral absorption coefficients of some porphyrins in the Soret band region (1960) Biochem J, 75, pp. 620-623 
504 |a Rossetti, Batlle, Polypyrrole intermediates in porphyrin biosynthesis (1977) Studies with Euglena gracilis, 8, pp. 277-283. , Int. J. Biochem 
504 |a Rossetti, Juknat, Batlle, Porphyrin biosynthesis in Euglena gracilis—II. Pyrrylmethane intermediates in the enzymic cyclotetramerization of porphobilinogen (1977) Int. J. Biochem., 8, pp. 781-787 
504 |a Rossetti, Juknat, Kotler, Fumagalli, Batlle, Occurrence of multiple molecular forms of porphobilinogenase in diverse organisms: the minimum quaternary structure of porphobilinogenase is a protomer of one deaminase and one isomerase domain (1980) Int. J. Biochem., 12, pp. 761-767 
504 |a Rossetti, Lombardo, Juknat, Araujo, Batlle, Porphyrin biosynthesis in Euglena gracilis—V. Soluble and particulate PBG-ase (1986) Comp. Biochem. Physiol., 85 B, pp. 451-458 
504 |a Sancovich, Batlle, Grinstein, The porphobilinogen deaminase-uroporphyrinogen III cosynthetase system (porphobilinogenase) from bovine liver (1969) Kinetic studies, 3, pp. 223-226. , FEBS Lett 
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504 |a Stella, Estudios sobre la enzima deltaaminolevúlico dehidrasa (1977) Doctoral thesis, , University of Buenos Aires, Argentine 
504 |a Wider, Batlle, del, Tigier, δ-Aminolaevulinate synthetase in extracts of cultured soybean callus (1971) Biochim. biophys. Acta, 253, pp. 511-517 
504 |a Williams, Morgan, McDonald, Battersby, Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kinetics (1981) Biochem. J., 193, pp. 301-310 
520 3 |a 1. 1. The effect of light and growing time on chlorophyll, protein content and the activity of porphobilinogenase (PBGase), in Euglena gracilis was studied. 2. 2. It was found that neither protein nor chlorophyll content or PBGase activity were dependent upon the days of growing or the light conditions of growth. 3. 3. Some properties of PBGase were studied. The addition of sodium and magnesium salts to the assay system did not modify enzyme activity. Uroporphyrinogen formation was linear with protein over a wide range of enzyme concentration. 4. 4. When activity was expressed on the basis of the amount of porphyrins formed an optimum pH of 7.4 was obtained but when it was expressed in terms of PBG consumed two pH maxima at 7.0 and 8.5 were observed. 5. 5. Direct plots of velocity against PBG concentration, when activity was measured as PBG consumed, were not hyperbolic; double-reciprocal plots were not linear and Hill plots gave a n value of 2, indicating the existence of positive co-operative effects between two binding sites for PBG per molecule of PBGase. © 1987.  |l eng 
536 |a Detalles de la financiación: Secretaria de Ciencia y Tecnica, Universidad de Buenos Aires 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Acknowledgemems--Maria Victoria Rossetti and Alcira M. del C. BatIle hold the post of Scicntific Researchcs in the Argentine National Council (CONICET); Maria ESsa Lombardo and Susana Correa Garcia are fclIows of CON~CET. This work was supported by grants from CONICET, SECYT, UBA, Secretaria de Salud ?fiblica dd Ministerio de Acddn SociaI y Medio Ambiente and ~anco de la Naci6n Argentina. The technical assistance of Mrs B. Ricillo de Aprea is gratefully acknowledged. 
593 |a Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), (CONICET-Facultad de Ciencias Exactas y Naturales, UBA) Ciudad Universitaria, Pabellón II 20 Piso, 1428 Buenos Aires Argentine, Argentina 
700 1 |a Araujo, L.S. 
700 1 |a Lombardo, M.E. 
700 1 |a García, S.C. 
700 1 |a del C. Batlle, A.M. 
773 0 |d 1987  |g v. 87  |h pp. 593-600  |k n. 3  |x 03050491  |w (AR-BaUEN)CENRE-2752  |t Comparative Biochemistry and Physiology -- Part B: Biochemistry and 
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