Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase

1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM...

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Autor principal: Navone, N.M
Otros Autores: Polo, C.F, Frisardi, A.L, M. del C. Batlle, A.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1991
Acceso en línea:Registro en Scopus
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LEADER 09301caa a22009977a 4500
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003 AR-BaUEN
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024 7 |2 scopus  |a 2-s2.0-0026078957 
024 7 |2 cas  |a Ammonia-Lyases, EC 4.3.1.; Hydroxymethylbilane Synthase, EC 4.3.1.8; porphobilinogenase, EC 5.-; Porphyrins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
100 1 |a Navone, N.M. 
245 1 0 |a Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase 
260 |c 1991 
270 1 0 |m M. del C. Batlle, A.; Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), CONICET-FCEN, UBA, Ciudad Universitaria, Pabellon II, 2do Piso, 1428 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Batlle, Rosetti, Enzymic polymerization of porphobilinogen into uroporphyrinogens—Review (1977) Int. J. Biochem., 8, pp. 251-267 
504 |a Batlle, Ferramola, Grinstein, Purification and general properties of delta-amino-laevulate dehydratase from cow liver (1967) Biochem. J., 104, pp. 244-249 
504 |a Batlle, Wider de Xifra, Stella, A simple method for measuring erythrocyte porphobilinogenase, and its use in the diagnosis of acute intermittent porphyria (1978) Int. J. Biochem., 9, pp. 871-876 
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 porphyrisn and related macrocycle Part 21 The interaction of deaminase and its products (hydroxymethylbilane) and the relationship between deaminase and cosynthetase (1983) Journal of the Chemical Society, Perkin Transactions 1, 1, pp. 3041-3047 
504 |a Bogorad, The enzymatic synthesis of porphyrins from porphobilinogen. I. Uroporphyrinogen I (1958) J. biol. Chem., 233, pp. 501-509 
504 |a Bogorad, The enzymatic synthesis of porphysins from porphobilinogen. II. Uroporphyrinogen III (1958) J. biol. Chem., 233, pp. 510-519 
504 |a Falk, Benson, Separation of uropophyrin esters I and III by paper chromatography (1953) Biochem. J., 55, pp. 101-107 
504 |a Fumagalli, (1988) Doctoral Thesis, , University of Buenos, Aires 
504 |a Fumagalli, Kotler, Rossetti, Batlle, Human red cell porphobilinogen deaminase A simpler method of purification and some unusual properties (1985) Int. J. Biochem., 17, pp. 485-489 
504 |a Hart, Abell, Battersby, Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthetase (porphobilinogen deaminase) from Escherichia coli (1986) Biochem.J., 240, pp. 273-276 
504 |a Jordan, Berry, Mechanism of action of porphobilinogen deaminase (1981) Biochem. J., 195, pp. 177-181 
504 |a Jordan, Burton, Nordlov, Schneider, Pryde, Scott, Pre-uroporphyrinogen a substrate for uroporphyrinogen III ocsynthetase (1979) Journal of the Chemical Society, Chemical Communications, pp. 204-205 
504 |a Jordan, Seehra, The biosynthesis of uroporphynnogen III. Order of assembly of the four porphobilinogen molecules in the formation of the tetrapyrrole ring (1979) FEBS Lett., 104, pp. 364-366 
504 |a Lowry, Rosebrough, Farr, Randall, Protein measurement with the Folin-phenol reagent (1951) J. biol. Chem., 193, pp. 265-275 
504 |a Llambías, Batlle, Porphyrin biosynthesis in soybean callus V The porphobilinogen deaminase—uroporphyrinogen III cosynthetase Kinetic studies (1970) Biochimica et Biophysica Acta (BBA) - Enzymology, 220, pp. 552-559 
504 |a Llambías, Batlle, Porphyrin biosynthesis VIII Avian erythrocyte porphobilinogen deaminse—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 Navone, Frisardi, Resnik, Batlle, Polo, Porphyrin biosynthesis in human breast cancer Preliminary mimetic in vitro studies (1988) Med. Sci. Res., 16, pp. 61-62 
504 |a Navone, Polo, Frisardi, Batlle, Heme enzyme pattern in mouse mammary carcinoma (1991) Int. J. Biochem., , (in press) 
504 |a Polo, Afonso, Batlle, Un método simplificado para la esterificación y la extracción de ésteres metílicos de porfirinas (1988) Acta Bioq. Clin. Latinoamer, 22, pp. 430-431 
504 |a Sancovich, Batlle, Grinstein, The porphobilinogen deaminase—uroporphyrinogen III cosynthetase system (porphobilinogenase) from bovine liver Kinetic studies (1969) FEBS Lett., 3, pp. 223-226 
504 |a Sassa, Zalar, Kappas, Studies in porphyria. VII. Induction of uroporphyrinogen I synthase and expression of the gene defect of acute intermittent porphyria in mitogen-stimulated human lymphocytes (1978) J. clin. Invest., 61, pp. 499-508 
504 |a Schoenfeld, Epstein, Klein, Lahav, Atsmon, The relation between porphobilinogen deaminase (PBGD) activity and growth (1985) lsr. J. Med. Sci., 21, pp. 870-871 
504 |a Stout, Becker, Heme enzyme patterns in genetically and chemically induced mouse liver tumors (1986) Cancer Res., 46, pp. 2756-2759 
504 |a Stout, Becker, Heme enzyme patterns in rat liver nodules and tumors (1987) Cancer Res., 47, pp. 963-966 
520 3 |a 1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM, Vmax of 1.57-1.83 nmol porphyrins/2 hr and a Hill coefficient of n = 1 were obtained for PBGase and Km values of 13 to 19 μM and Vmax of 2.6-4.8 were obtained for HMB-S. 3. 3. Porphyrin synthesis was linear up to 180 min of incubation in all cases for PBGase and HMB-S, and greatly increased with higher incubation temperature being maximal at 60°C and nil at 70°C, optimal temperature was 37°C for either enzyme in either source. 4. 4. Uroporphyrinogen III synthetase was heat inactivated while HMB-S was a heat stable enzyme. Optimum pH was 8.2 for PBGase and HMB-S in either tissue. © 1991.  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Acknowledgements--This work was supportedb y grants from the CONICET, UBA and Banco de la Naci6n Argentina.A . L. Frisardi is grateful to Laboratorios PROMECO for a fellowshipW. e thankD r N. Andradea nd Dr S. Bonapartefr, omthe InstitutoN ationadl eOncologia "Angel H. Roffo", for providingu s with the originalt umor specimenfso r transplantatioann,d Joy Ricciardif or some chemicalsW. e are mostg ratefutlo Lic S. G. Afonso for the excellendt rawing. A. M. del C. Batlleh oldst hepost of SuperiorS cientific Researcheinr the CONICET. N. Navonea ndC. Polo are Researcha ssistantast the CONICET. A. M. del C. Batlle also thankst heM inisteriod e Educacitny Ciencia( MEC), Spain and the Association for InternationaCl ancer Research( AICR), United Kingdom for specials upport. 
593 |a Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), CONICET-FCEN, UBA, Ciudad Universitaria, Pabellon II, 2do Piso, 1428 Buenos Aires, Argentina 
690 1 0 |a PORPHOBILINOGEN DEAMINASE 
690 1 0 |a PORPHOBILINOGENASE 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a UROPORPHYRINOGEN III SYNTHASE 
690 1 0 |a ANIMAL TISSUE 
690 1 0 |a ARTICLE 
690 1 0 |a BREAST ADENOCARCINOMA 
690 1 0 |a LIVER 
690 1 0 |a MALE 
690 1 0 |a MOUSE 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a AMMONIA-LYASES 
690 1 0 |a ANIMAL 
690 1 0 |a HYDROGEN-ION CONCENTRATION 
690 1 0 |a HYDROXYMETHYLBILANE SYNTHASE 
690 1 0 |a KINETICS 
690 1 0 |a LIVER 
690 1 0 |a MALE 
690 1 0 |a MAMMARY NEOPLASMS, EXPERIMENTAL 
690 1 0 |a MICE 
690 1 0 |a MICE, INBRED BALB C 
690 1 0 |a NEOPLASM TRANSPLANTATION 
690 1 0 |a PORPHYRINS 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
690 1 0 |a TEMPERATURE 
690 1 0 |a ANIMALIA 
700 1 |a Polo, C.F. 
700 1 |a Frisardi, A.L. 
700 1 |a M. del C. Batlle, A. 
773 0 |d 1991  |g v. 98  |h pp. 67-71  |k n. 1  |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_v98_n1_p67_Navone  |y Handle 
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