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Abstract:

1. 1. Gel filtration on Sephadex G-100 and Sepharose 4B were used to redetermine the molecular weight (MW) of porphobilinogenase, deaminase and isomerase purified from different sources, and determine the MW of these enzymes purified from Eugtena gracilis. 2. 2. Results reported here, indicate that porphobilinogenase can be found, into three different molecular forms, tetramers, dimers and monomers according to the source organism. 3. 3. It is proposed that minimal functional structure of PBGase is a hybrid protomer of MW 25,000, composed by two different domains, in a ratio of 1 mol of deaminase, MW 20,000 to 1 mol of isomerase. MW 5000. 4. 4. A model explaining the occurrence of different MW species of PBGase in nature and the possible interconversion among the various forms is postulated. © 1980.

Registro:

Documento: Artículo
Título: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
Autor:Rossetti, M.V.; de Geralnik, A.A.J.; Kotler, M.; Fumagalli, S.; del C. Batlle, A.M.
Filiación:Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellon II, 4Piso, Nüñez, 1428 Buenos Aires, Argentina
Palabras clave:ammonia lyase; Ammonia Lyases; hydrolase; isomerase; multienzyme complex; animal; article; bird; cattle; comparative study; enzymology; erythrocyte; Euglena gracilis; isolation and purification; liver; macromolecule; molecular weight; plant; protein conformation; species difference; Aminohydrolases; Ammonia-Lyases; Animal; Birds; Cattle; Comparative Study; Erythrocytes; Euglena gracilis; Isomerases; Liver; Macromolecular Systems; Molecular Weight; Multienzyme Complexes; Plants; Protein Conformation; Species Specificity; Support, Non-U.S. Gov't
Año:1980
Volumen:12
Número:5-6
Página de inicio:761
Página de fin:767
DOI: http://dx.doi.org/10.1016/0020-711X(80)90159-7
Título revista:International Journal of Biochemistry
Título revista abreviado:Int. J. Biochem.
ISSN:0020711X
CODEN:IJBOB
CAS:hydrolase, 9027-41-2; isomerase, 9013-19-8; Aminohydrolases, EC 3.5.4.; Ammonia-Lyases, EC 4.3.1.; Isomerases, EC 5.; Macromolecular Systems; Multienzyme Complexes
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_0020711X_v12_n5-6_p761_Rossetti.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p761_Rossetti

Referencias:

  • Batlle A.M. del, Estimation of molecular weights of proteins by Bio-gel P gel filtration (1967) Journal of Chromatography A, 8, pp. 82-88
  • Batlle A.M. del, Rossetti, Review—Enzymic polymerization of porphobilinogen into uroporphyrinogens (1977) Int. J. Biochem., 8, pp. 251-267
  • Batlle A.M. del, Benson, Rimington, Purification and properties of Coproporphyrinogenase (1965) Biochem. J., 97, pp. 731-740
  • Frydman, Feinstein, Studies on porphobilinogen deaminase and uroporphyrinogen III. Cosynthetase from human erythrocytes (1974) Biochim. biophys. Acta, 350, pp. 358-373
  • Higuchi, Bogorad, The purification and properties of uroporphyrinogen I synthases and uroporphyrinogen III cosynthetase. Interactions between the enzymes (1975) Ann. N.Y. Acad. Sci., 244, pp. 401-418
  • Jordan, Shemin, Purification of uroporphyrinogen I synthetase from R. spheroides (1973) J. biol. Chem., 243, pp. 1019-1024
  • Kreutzer, Schmidt, Stadler, Zeitler, Purification and characterization of animal porphobilinogen synthetases I. Bovine liver porphobilinogen synthetase (1977) Hoppe-Seyler's Z. Physiol. Chem., 358, pp. 1081-1091
  • Llambias, Batlle A.M. del, Studies on the porphobilinogen deaminase-uroporphyrinogen cosynthetase system of cultured soyabean cells (1971) Biochem J, 121, pp. 327-340
  • Llambias, Batlle A.M. del, 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
  • Locascio, Tigier, Batlle A.M. del, Estimation of molecular weights of protein by agarose filtration (1969) J. Chromat., 40, pp. 453-457
  • Lowry, Rosebrough, Farr, Randall, Protein measurements with the folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275
  • Rossetti, Batlle A.M. del, Polypyrrole intermediates in porphyrin biosynthesis—studies with Euglena gracilis (1977) Int. J. Biochem., 8, pp. 277-283
  • Rossetti, Juknat de Geralnik, Batlle A.M. del, (1980) Porphyrin biosynthesis in Euglena gracilis III. Studies on the isolation and purification of the enzymes involved in the ciclotetramerization of porphobilinogen, , In preparation
  • Sancovich, Batlle A.M. del, Grinstein, Porphyrin biosynthesis VI. Separation and purification of porphobilinogen deaminase and uroporphyrinogen isomerase from cow liver porphobilinogenase, an allosteric enzyme (1969) Biochim. biophys. Acta, 191, pp. 130-143
  • Sancovich, Ferramola, Batlle A.M. del, Kivilevich, Grinstein, Studies on cow liver porphobilinogen deaminase (1976) Acta Physiol., 26, pp. 379-386

Citas:

---------- APA ----------
Rossetti, M.V., de Geralnik, A.A.J., Kotler, M., Fumagalli, S. & del C. Batlle, A.M. (1980) . 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. International Journal of Biochemistry, 12(5-6), 761-767.
http://dx.doi.org/10.1016/0020-711X(80)90159-7
---------- CHICAGO ----------
Rossetti, M.V., de Geralnik, A.A.J., Kotler, M., Fumagalli, S., del C. Batlle, A.M. "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" . International Journal of Biochemistry 12, no. 5-6 (1980) : 761-767.
http://dx.doi.org/10.1016/0020-711X(80)90159-7
---------- MLA ----------
Rossetti, M.V., de Geralnik, A.A.J., Kotler, M., Fumagalli, S., del C. Batlle, A.M. "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" . International Journal of Biochemistry, vol. 12, no. 5-6, 1980, pp. 761-767.
http://dx.doi.org/10.1016/0020-711X(80)90159-7
---------- VANCOUVER ----------
Rossetti, M.V., de Geralnik, A.A.J., Kotler, M., Fumagalli, S., del C. Batlle, A.M. 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. Int. J. Biochem. 1980;12(5-6):761-767.
http://dx.doi.org/10.1016/0020-711X(80)90159-7