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Sorianello, E.M.; Mazzetti, M.B. "Function and structure of rat hepatic coproporphyrinogen oxidase" (2000) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 127(2):155-164
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Abstract:

Rat hepatic coproporphyrinogen oxidase, the sixth enzyme in the heme biosynthetic pathway, was purified 1340-fold with a yield of 39.7%. To obtain the soluble enzyme, different methods were applied to disrupt mitochondria, with sonication giving the highest yield (85%). The minimum catalytic form of enzyme was a dimer with a molecular mass of 77±4 kDa. The existence of aggregated forms was possible since in fractions of gel filtration elution activity was observed with higher molecular mass. We determined a Stokes radius of 36.3 A, a sedimentation coefficient (S20,(w)) of 5.06 S, and frictional ratio of 1.29, suggesting a nearly globular shape of the protein. Regardless of the type of salt, high ionic strength inhibits the enzyme, probably modifying its native structure. Experiments with amino acid modifiers showed that histidine, arginine, and tryptophan are involved in the catalytic process. Non-ionic detergents and phospholipids activated the enzyme, probably because they reproduce its natural hydrophobic environment. The present study describes a simple method for the purification of rat liver coproporphyrinogen oxidase, introducing for the first time data on the structure and function of the protein in a tissue often used as a laboratory model in biological studies, and contributing to the study of human hereditary coproporphyria. Copyright (C) 2000 Elsevier Science Inc.

Registro:

Documento: Artículo
Título:Function and structure of rat hepatic coproporphyrinogen oxidase
Autor:Sorianello, E.M.; Mazzetti, M.B.
Filiación:Depto. de Qulmica Biológica, Fac. de Ciencias Exactas y Naturales, 2do. Pabellón, (1428) Buenos Aires, Argentina
Departmento 12, Medrano 375, Capital Federal, (1178) Buenos Aires, Argentina
Palabras clave:Amino acid modifiers; Catalytic activity; Coproporphyria; Coproporphyrin; Coproporphyrinogen oxidase; Enzyme; Protoporphyrin IX; Protoporphyrinogen IX; Purification; Rat liver; coproporphyrin; coproporphyrinogen oxidase; protoporphyrinogen oxidase; amino acid sequence; animal experiment; animal tissue; article; controlled study; coproporphyria; enzyme activity; enzyme purification; enzyme structure, function and variability; liver metabolism; molecular weight; nonhuman; priority journal; rat; Animals; Chromatography, High Pressure Liquid; Coproporphyrinogen Oxidase; Detergents; Diethyl Pyrocarbonate; Humans; Liver; Octoxynol; Phenylglyoxal; Phospholipids; Polysorbates; Rats; Rats, Sprague-Dawley; Water
Año:2000
Volumen:127
Número:2
Página de inicio:155
Página de fin:164
DOI: http://dx.doi.org/10.1016/S0305-0491(00)00247-9
Título revista:Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Título revista abreviado:Comp. Biochem. Physiol. B Biochem. Mol. Biol.
ISSN:03050491
CODEN:CBPBB
CAS:Coproporphyrinogen Oxidase, EC 1.3.3.3; Detergents; Diethyl Pyrocarbonate, 1609-47-8; Octoxynol, 9002-93-1; Phenylglyoxal, 1074-12-0; Phospholipids; Polysorbates; Water, 7732-18-5
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v127_n2_p155_Sorianello

Referencias:

  • Andrews, P., Estimation of molecular size and molecular weights of biological compounds gel filtration (1970) Methods Biochem. Anal., 18, pp. 1-53
  • Battle, A.M., Del, C., Benson, A., Reminngton, C., Purification and properties of coproporphyrinogenase (1965) Biochem. J., 97, pp. 731-740
  • Bogard, M., Camadro, J.M., Nordman, Y., Labbe, P., Purification and properties of mouse liver coproporphyrinogen oxidase (1989) Eur. J. Biochem., 181, pp. 417-421
  • Cacheux, V., Martásek, P., Fougerousse, F., Delfau, M., Druart, L., Tachdjian, G., Grandchamp, B., Localization of the human coproporphyrinogen oxidase gene to chromosome band 3q12 (1994) Hum. Genet., 94, pp. 557-559
  • Camadro, J.M., Chambon, H., Jolles, J., Labbé, P., Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae (1986) Eur. J. Biochem., 156, pp. 576-587
  • Dailey, H.A., Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: Terminal three enzymes (1990) Biosythnesis of Heme and Chlorophyll, pp. 123-161. , Dailey, H.A. (Ed.), McGraw-Hill, New York
  • Elder, G.H., Evans, J.O., Jackson, J.R., Jackson, A.H., Factors determining the sequence of oxidative decarboxylation of the 2- and 4-propianate substituents of coproporphyrinogen III coproporphyrinogen oxidase in rat liver (1978) Biochem. J., 169, pp. 215-223
  • Falk, J.E., (1964) Porphyrins and Metalloporphyrins, , Elsevier, Amsterdam
  • Grandchamp, B., Phung, N., Nordmann, Y., The mitochondrial localization of coproporphyrinogen III oxidase (1978) Biochem. J., 176, pp. 97-102
  • Jones, M.A., Hamilton, M.L., Lash, T.D., Effect of covalent modification on coproporphyrinogen oxidase from chicken red blood cells (1997) Prep. Biochem. Biotechnol., 27, pp. 47-57
  • Kappas, A., Sassa, S., Galbraith, R.A., Nordmann, Y., The Porphyrias. Hereditary Coproporphyria (1995) Metabolic and Molecular Bases of Inherited Disease, pp. 2135-2155. , Scriver, C.R., Beaudet, A.L., Sly, W.S., Valle, D., Stanbury, J.B., Wyngaarden, J.B., Fredickson, D.S. (Eds.), McGraw-Hill, New York
  • Kohno, H., Furukawa, T., Tokunaga, R., Taketani, S., Yoshinaga, T., Mouse coproporphyrinogen oxidase is a copper-containing enzyme: Expression in Escherichia coli and site-directed mutagenesis (1996) Biochim. Biophys. Acta, 1292, pp. 156-162
  • Kohno, H., Furukawa, T., Yoshinaga, T., Tokunaga, R., Taketani, S., Coproporphyrinogen oxidase. Purification, molecular cloning and induction of mRNA during erythroid differentiation (1993) J. Biol. Chem., 268, pp. 21359-21363
  • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (London), 227, pp. 680-685
  • Lamoril, J., Deybach, J.C., Puy, H.O., Grandchamp, B., Nordmann, Y., Three novel mutations in the coproporphyrinogen oxidase gen (1997) Hum. Mutat., 9, pp. 78-80
  • Laurent, T.C., Killander, J.A., Theory of gel filtration and its experimental verification (1964) J. Chromatogr., 14, pp. 317-330
  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurements with the Folin phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275
  • Martásek, P., Camadro, J., Delfau-Larue, M., Dumas, J., Montagne, J., De Verneuil, H., Labbé, P., Grandchamp, B., Molecular cloning sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase (1994) Proc. Natl. Acad. Sci., 91, pp. 3024-3028
  • Martásek, P., Camadro, J.M., Raman, C.S., Lecomte, M.C., Le Caer, J.P., Demeler, B., Grandchamp, B., Labbé, P., Human coproporphyrinogen oxidase. Biochemical characterization of recombinant normal and R231W mutated enzyme expressed in E. coli as soluble, catalytically active homodimers (1997) Cell. Mol. Biol., 43, pp. 47-58
  • Mazzetti, M.B., Tomio, J.M., Studies on the catalytic activity of human hepatic porphobilinogen deaminase (1997) Biochem. Mol. Biol. Internat., 42, pp. 685-692
  • Martin, R.G., Ames, B.N., A method for determining the sedimentation behavior of enzymes: Application to protein mixture (1961) J. Biol. Chem., 236, pp. 1372-1379
  • Medlock, A.E., Dailey, H.A., Human coproporphyrinogen oxidase is not a metalloprotein (1996) J. Biol. Chem., 271, pp. 32507-32510
  • Metzler, D.E., Biochemistry (1977) The Chemical Reactions of Living Cells, pp. 250-255. , Academic Press, New York
  • Miles, E.W., Modification of histidyl residues in proteins by diethylpyrocarbonate (1977) Methods of Enzymology. Enzyme Structure, 47 (PART E), pp. 431-442. , Hirs, C.H.W., Timasheff, S.N. (Eds.), Academic Press, New York
  • Ochs, D.E., McConkey, E.H., Sammons, D.W., Silver stain for proteins in polyacrylamide gels: A comparison of six methods (1981) Electrophoresis, 2, pp. 304-307
  • Poulson, R., Polglase, W.J., Aerobic and anaerobic coproporphyrinogenase activities in extracts from Sacharomyces cerevisiae (1974) J. Biol. Chem., 249, pp. 6367-6371
  • Riordan, F.F., MacElvany, K.D., Arginyl residues: Anion recognition sites in enzymes (1977) Science, 195, pp. 884-886
  • Rosipal, R., Lamoril, J., Puy, H., Da Silva, V., Gouya, L., De Rooij, F.W., Te Velde, K., Deybach, J.C., Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation uptade (1999) Hum. Mutat., 13, pp. 44-53
  • Siegel, L.M., Monti, K.Y., Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite hydroxilamine reductases (1966) Biochim. Biophys. Acta, 112, pp. 346-362
  • Sorianello, E.M., (1998) Caracterización Estructural Y Funcional de la Enzima Coproporfirinogeno Oxidasa Hepática de Mamíferos, pp. 23-27. , Thesis. Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires
  • Spande, T.F., Green, N.M., Witkop, B., The reactivity towards N-bromosuccinimide of tryptophan in enzymes, zymogens, and inhibited enzymes (1966) Biochemistry, 5, pp. 1923-1926
  • Spande, T.F., Witkop, B., Chemical evidence for involvement of tryptophan in the interaction of trysin with the inhibitor from beef pancreas (1965) Biochem. Biophys. Res. Commun., 26, pp. 131-134
  • Takahashi, K., The reaction of phenylglyoxal with arginine residues in protein (1968) J. Biol. Chem., 23, pp. 6171-6179
  • Taketani, S., Kohno, H., Furukawa, T., Yoshinaga, T., Tocunaga, R., Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase (1994) Biochim. Biophys. Acta, 1183, pp. 547-549
  • Yoshinaga, T., Sano, S., Coproporphyrinogen oxidase. I. Purification, properties, and activation by phospholipids (1980) J. Biol. Chem., 255, pp. 4722-4726
  • Yoshinaga, T., Sano, S., Coproporphyrinogen oxidase. II. Reaction mechanism and role of ty-rosine residues on the activity (1980) J. Biol. Chem., 255, pp. 4727-4731
  • Witkop, B., Buried and exposed tryptophan in tobacco mosaic virus (TMV) protein (1961) Adv. Protein Chem., 16, pp. 285-289. , Anfinsen, C.B. Jr., Bailey, K., Anson, M.L., Edsall, J.T. (Eds.), Academic Press, New York and London

Citas:

---------- APA ----------
Sorianello, E.M. & Mazzetti, M.B. (2000) . Function and structure of rat hepatic coproporphyrinogen oxidase. Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 127(2), 155-164.
http://dx.doi.org/10.1016/S0305-0491(00)00247-9
---------- CHICAGO ----------
Sorianello, E.M., Mazzetti, M.B. "Function and structure of rat hepatic coproporphyrinogen oxidase" . Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology 127, no. 2 (2000) : 155-164.
http://dx.doi.org/10.1016/S0305-0491(00)00247-9
---------- MLA ----------
Sorianello, E.M., Mazzetti, M.B. "Function and structure of rat hepatic coproporphyrinogen oxidase" . Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, vol. 127, no. 2, 2000, pp. 155-164.
http://dx.doi.org/10.1016/S0305-0491(00)00247-9
---------- VANCOUVER ----------
Sorianello, E.M., Mazzetti, M.B. Function and structure of rat hepatic coproporphyrinogen oxidase. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2000;127(2):155-164.
http://dx.doi.org/10.1016/S0305-0491(00)00247-9