Porphobilinogenase from Rhodopseudomonas palustris
1. 1. Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the am...
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1989
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| LEADER | 10540caa a22010457a 4500 | ||
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| 001 | PAPER-677 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203001.0 | ||
| 008 | 190411s1989 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0024534681 | |
| 024 | 7 | |2 cas |a porphobilinogenase, 9055-40-7; Ammonia-Lyases, EC 4.3.1.; porphobilinogenase, EC 5.- | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Juknat, A.A. | |
| 245 | 1 | 0 | |a Porphobilinogenase from Rhodopseudomonas palustris |
| 260 | |c 1989 | ||
| 270 | 1 | 0 | |m Batlle, A.M.d.C.; Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (FCEN, UBA-CONICET), Ciudad Universitaria, Pabellon II, 2do. Piso, 1428 Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Batlle, Estimation of molecular weights of proteins by bio-gel P gel filtration (1967) Journal of Chromatography A, 8, pp. 82-88 | ||
| 504 | |a Battersby, Fookes, Gustafson-Potter, McDonald, Matcham, Biosynthesis of porphyries and related macrocycles. Part 17. 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, Hart, Matcham, Pandey, Biosynthesis of porphyrins and related macrocycles. Part 21. The interaction of deaminase and its product (hydroxymethylbilane) and the relationship between deaminase and cosynthetase (1983) Journal of the Chemical Society, Perkin Transactions 1, 1, pp. 3041-3047 | ||
| 504 | |a Battersby, Fookes, Matcham, McDonald, Gustafson-Potter, Biosynthesis of the natural porphyrins: experiments on the ring-closure steps and with the hydroxy-analogue of porphobilinogen (1979) Journal of the Chemical Society, Chemical Communications, pp. 316-319 | ||
| 504 | |a Battersby, Fookes, Matcham, McDonald, Order of assembly of the four pyrrole rings during biosynthesis of the natural porphyrins (1979) Journal of the Chemical Society, Chemical Communications, pp. 539-541 | ||
| 504 | |a Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Analyt. Biochem., 72, pp. 248-254 | ||
| 504 | |a Burton, Fagerness, Hosozawa, Jordan, Scott, 13C-NMR evidence for a new intermediate, pre-uroporphyrinogen, in the enzymic transformation of porphobilinogen into uroporphyrinogens I and III (1979) Journal of the Chemical Society, Chemical Communications, pp. 202-204 | ||
| 504 | |a Clement, Kohashi, Piper, Rat hepatic uroporphyrinogen III cosynthetase: Purification, properties and inhibition by metal ions (1982) Archs Biochem. Biophys., 214 (2), pp. 657-667 | ||
| 504 | |a Cohen-Bazire, Sistrom, Stanier, Kinetic studies of pigment synthesis by non-sulfur purple bacteria (1957) J. cell comp. Physiol., 49, pp. 25-68 | ||
| 504 | |a Davies, Neuberger, Polypyrroles formed from porphobilinogen and amines by uroporphyrinogen synthetase of Rhodopseudomonas spheroides (1973) Biochem. J., 133, pp. 471-492 | ||
| 504 | |a Frydman, Frydman, Tomaro, Pyrroloxygenases: a new type of oxidases (1973) Molec. cell. Biochem., 2 (2), pp. 121-136 | ||
| 504 | |a Frydman, Tomaro, Wanschelbaum, Andersen, Awruch, Frydman, Porphobilinogen from wheat germ: isolation, properties and products formed (1973) Biochemistry, 12 (26), pp. 5253-5262 | ||
| 504 | |a Fumagalli, Rossetti, Juknat, Kotler, Batlle, Estudios sobre la PBG-asa de higado de cerdo (1982) An. Asoc. quím. argent., 70, pp. 375-382 | ||
| 504 | |a Heath, Hoare, The biosynthesis of porphyrins from porphobilinogen by Rhodopseudomonas spheroides (1959) Biochem. J., 72, pp. 14-22 | ||
| 504 | |a Hoare, Heath, The biosynthesis of porphyrins from porphobilinogen by Rhodopseudomonas spheroides (1959) Biochem. J., 73, pp. 679-690 | ||
| 504 | |a Jordan, Burton, Nordlov, Schneider, Pryde, Scott, Pre-uroporphyrinogen: a substrate for uroporphyrinogen III cosynthetase (1979) Journal of the Chemical Society, Chemical Communications, pp. 204-205 | ||
| 504 | |a Jordan, Shemin, Purification and properties of uroporphyrinogen I synthetase from Rhodopseudomonas spheroides. (1973) J Biol Chem, 248, pp. 1019-1024 | ||
| 504 | |a Juknat, Biosynthesis of porphyrinogens (1983) Ph.D. Thesis, , University of Buenos Aires, Argentina | ||
| 504 | |a Keilin, Hartree, Purification of horse radish peroxidase and comparison of its properties with those of catalase and methaemoglobin (1951) Biochem. J., 49, pp. 88-104 | ||
| 504 | |a Kotler, Fumagalli, Juknat, Batlle, Porphyrin biosynthesis in Rp. palustris—VIII. Purification and properties of deaminase (1987) Comp. Biochem. Physiol., 87 B, pp. 601-606 | ||
| 504 | |a Kotler, Fumagalli, Juknat, Batlle, Porphyrin biosynthesis in Rp. palustris—IX. PBG-deaminase (1987) Kinetic studies, 19, pp. 981-985. , Int. J. Biochem., (10) | ||
| 504 | |a Levin, Uroporphyrinogen III cosynthetase from mouse spleen (1968) Biochemistry, 7 (11), pp. 3781-3788 | ||
| 504 | |a Levin, Enzymatic properties of uroporphyrinogen III cosynthetase (1971) Biochemistry, 10 (25), pp. 4669-4675 | ||
| 504 | |a Llambias, Batlle, Studies on the porphobilinogen deaminase-uroporphyrinogen cosynthetase system of cultured soya-bean cells. (1971) Biochem J, 121, pp. 327-340 | ||
| 504 | |a Llambias, Batlle, Porphyrin biosynthesis. VIII. Avian erythrocyte porphobilinogen deaminase-uroporphyrinogen III cosynthetase, its purification, properties and the separation of its components (1971) Biochimica et Biophysica Acta (BBA) - Enzymology, 227, pp. 180-191 | ||
| 504 | |a Lockwood, Rimington, Purification of an enzyme converting porphobilinogen to uroporphyrinogen (1957) Biochem. J., 67, pp. 8-11 | ||
| 504 | |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275 | ||
| 504 | |a Moore, Labbe, Assays for ALA and PBG determination (1964) Clin. Chem., 10, pp. 1105-1109 | ||
| 504 | |a Rimington, Spectral-absorption coefficients of some porphyrins in the Soret-band region. (1960) Biochem J, 75, pp. 620-623 | ||
| 504 | |a Rossetti, Enzymic cyclotetramerization of PBG (1978) Its mechanism, , Ph.D. Thesis, University of Buenos Aires, Argentina | ||
| 504 | |a Rossetti, Lombardo, Juknat de Geralnik, Araujo, Batlle, Porphyrin biosynthesis in Euglena gracilis—V. Soluble and particulate PBG-ase (1986) Comp. Biochem. Physiol., 85 B, pp. 451-458 | ||
| 504 | |a Rossetti, Araujo, Lombardo, Correa Garcia, Batlle, Porphyrin biosynthesis in Euglena gracilis—VI. The effect of light and growth conditions on PBG-ase activity and further properties (1987) Comp. Biochem. Physiol., 87 B, pp. 593-600 | ||
| 504 | |a Sancovich, Batlle, Grinstein, Porphyrin biosynthesis—VI. Separation and purification of PBG-deaminase and uroporphyrinogen isomerase from cow liver (1969) PBG-ase an allosteric enzyme, 191, pp. 130-143. , Biochim. biophys. Acta | ||
| 504 | |a Tomaro, Frydman, Frydman, Porphobilinogen oxygenase from rat liver: induction, isolation and properties (1973) Biochemistry, 12 (26), pp. 5263-5268 | ||
| 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. Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the amount of PBG consumed. 3. 3. Cyclotetramerization rate and distribution of reaction products were not affected either by the presence or absence of oxygen. 4. 4. Two PBGase active species of mol. wt 115,000 and 50,000 were found, by means of gel filtration through a calibrated Sephadex G-100 column. 5. 5. Kinetic data show the existence of positive cooperative effects for porphyrin formation, while a hyperbolic behaviour for PBG consumption was observed. © 1989. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Secretaria de Ciencia y Tecnica, Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: National Council for Scientific Research | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Acknowledgements This work was supported by grants from the CONICET (Argentine National Research Council), SECYT, Secretaria de Salud Publica del Minis-terio de Salud Publica, Banco de la Nacion Argentina and the University of Buenos Aires. | ||
| 593 | |a Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (FCEN, UBA-CONICET), Ciudad Universitaria, Pabellon II, 2do. Piso, 1428 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a AMMONIA LYASE |
| 690 | 1 | 0 | |a AMMONIA LYASES |
| 690 | 1 | 0 | |a PORPHOBILINOGENASE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a ENZYMOLOGY |
| 690 | 1 | 0 | |a GEL CHROMATOGRAPHY |
| 690 | 1 | 0 | |a ISOLATION AND PURIFICATION |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a RHODOPSEUDOMONAS |
| 690 | 1 | 0 | |a AMMONIA-LYASES |
| 690 | 1 | 0 | |a CHROMATOGRAPHY, GEL |
| 690 | 1 | 0 | |a HYDROGEN-ION CONCENTRATION |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a RHODOPSEUDOMONAS |
| 690 | 1 | 0 | |a SUPPORT, NON-U.S. GOV'T |
| 650 | 1 | 7 | |2 spines |a PH |
| 700 | 1 | |a Kotler, M.L. | |
| 700 | 1 | |a Koopmann, G.E. | |
| 700 | 1 | |a Batlle, A.M.d.C. | |
| 773 | 0 | |d 1989 |g v. 92 |h pp. 291-295 |k n. 2 |x 03050491 |w (AR-BaUEN)CENRE-2752 |t Comparative Biochemistry and Physiology -- Part B: Biochemistry and | |
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| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_03050491_v92_n2_p291_Juknat |y Handle |
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