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Abstract:

1. 1. By chromatography through Sephadex G-200 of increasing amounts of partially purified pig liver ALA-D, different profiles were obtained, showing that species of molecular weights ranging from 140,000 to 560,000 might exist in equilibrium, but their relative ratio was dependent on the total amount of protein sampled. In all cases, however, the main peak (60-70%) corresponded to the 280,000 MW oligomer, that is the octamer. 2. 2. It was found that elution profiles were also dependent on column dimensions and on the purity of the enzyme preparation. 3. 3. K+ ions affected both catalytic activity and aggregation of the enzyme. 4. Results here reported add further support to the proposal of the existence of a minimal functional dimer. © 1980.

Registro:

Documento: Artículo
Título:Influencing its molecular weight determination
Autor:Stafforini, D.M.; Polo, C.F.; Stella, A.M.; De Xifra, E.W.; 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, 4. Piso, Nüñez1428, Argentina
Palabras clave:porphobilinogen synthase; potassium; animal; article; enzymology; isolation and purification; liver; macromolecule; metabolism; molecular weight; swine; Animal; Liver; Macromolecular Systems; Molecular Weight; Porphobilinogen Synthase; Potassium; Support, Non-U.S. Gov't; Swine
Año:1980
Volumen:12
Número:5-6
Página de inicio:757
Página de fin:760
DOI: http://dx.doi.org/10.1016/0020-711X(80)90158-5
Título revista:International Journal of Biochemistry
Título revista abreviado:Int. J. Biochem.
ISSN:0020711X
CODEN:IJBOB
CAS:porphobilinogen synthase, 9036-37-7; potassium, 7440-09-7; Macromolecular Systems; Porphobilinogen Synthase, EC 4.2.1.24; Potassium, 7440-09-7
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_0020711X_v12_n5-6_p757_Stafforini.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p757_Stafforini

Referencias:

  • del Batlle, Estimation of molecular weights of proteins by Bio GelP gel filtration (1967) Journal of Chromatography A, 28, pp. 82-88
  • del Batlle, Chromatografia con tamices moleculares (1968) Cienc. Invest., 24, pp. 242-261
  • del Batlle, Stella, Delta Aminolaevulinate Dehydratase. Its mechanism of action (1978) Int. J. Biochem., 9, pp. 861-864
  • Batlle A.M. Del, Benson, Riminoton, Purification and properties of Coproporphyrinogenase (1965) Biochem. J., 97, pp. 731-740
  • Batlle A.M. Del, Ferramola, Grinstein, Purification and general properties of deltaaminolaevulate dehydratase from cow liver (1967) Biochem. J., 104, pp. 244-249
  • del Batlle, Stella, Ferramola, Sopena, Wider, Sancovich, Porphyrin biosynthesis—immobilized enzymes and ligands X. A novel approach to the study of the relationship between the quaternary structure of aminolevulinate dehydratase and its activity (1978) Int. J. Biochem., 9, pp. 401-406
  • Calissano, Bonsionore, Cartasegna, Control of haem synthesis by feed back inhibition on human erythrocyte delta ALA-dehydratase (1966) Biochem. J., 101, pp. 550-555
  • Coleman, Purification and properties of deltaaminolevulinic acid dehydratase from tissues of two strains of mice (1966) J. biol. Chem., 241, pp. 5511-5520
  • Gurne, Chen, Shemin, Dissociation and reassociation of immobilized porphobilinogen synthase. use of immobilized subunits for enzyme isolation (1977) Proc. Natn Acad. Sci. U.S.A., 74, pp. 1383-1387
  • Locascio, Tigier, del Batlle, Estimation of molecular weights of proteins by agarose gel filtration (1969) J. Chromat., 40, pp. 453-457
  • Lowry, Rosenbrough, Farr, Randall, Protein measurement with the folin phenol reagent (1951) J. biol. Chem., 193, pp. 265-275
  • Nandi, Shemin, Delta-ALA-dehydratase of Rh. spheroides II. Association to polymers and dissociation to subunits (1968) J. biol. Chem., 243, pp. 1231-1235
  • Nandi, Shemin, Delta-ALA-dehydratase of Rh. spheroides III. Mechanism of porphobilinogen synthesis (1968) J. biol. Chem., 243, pp. 1236-1240
  • Polo, Stafforini, Stella, Wider, del Batlle, (1980) Pig liver aminolevulinate dehydratase I. Alternative methods for its purification and properties of the enzyme, , In preparation
  • Shemin, gd-Aminolevulinic acid dehydratase (1972) The Enzyme, 7, pp. 323-337. , Academic Press, NY, London
  • Tigier, del Batlle, Locascio, Porphyrin biosynthesis in soybean callus tissue III. Improved purification and some properties of delta aminolaevulinate dehydratase (1970) Enzymology, 38, pp. 43-56
  • Van Heyningen, Shemin, Quaternary structure of δ-aminolevulinate dehydratase from Rh. spheroides (1971) Biochemistry, 10, pp. 4676-4682
  • Wu, Shemin, Richards, Williams, The quaternary structure of δ-aminolevulinic acid dehydratase from bovine liver (1974) Proc. Natn Acad. Sci. U.S.A., 71, pp. 1767-1770

Citas:

---------- APA ----------
Stafforini, D.M., Polo, C.F., Stella, A.M., De Xifra, E.W. & Del C. Batlle, A.M. (1980) . Influencing its molecular weight determination. International Journal of Biochemistry, 12(5-6), 757-760.
http://dx.doi.org/10.1016/0020-711X(80)90158-5
---------- CHICAGO ----------
Stafforini, D.M., Polo, C.F., Stella, A.M., De Xifra, E.W., Del C. Batlle, A.M. "Influencing its molecular weight determination" . International Journal of Biochemistry 12, no. 5-6 (1980) : 757-760.
http://dx.doi.org/10.1016/0020-711X(80)90158-5
---------- MLA ----------
Stafforini, D.M., Polo, C.F., Stella, A.M., De Xifra, E.W., Del C. Batlle, A.M. "Influencing its molecular weight determination" . International Journal of Biochemistry, vol. 12, no. 5-6, 1980, pp. 757-760.
http://dx.doi.org/10.1016/0020-711X(80)90158-5
---------- VANCOUVER ----------
Stafforini, D.M., Polo, C.F., Stella, A.M., De Xifra, E.W., Del C. Batlle, A.M. Influencing its molecular weight determination. Int. J. Biochem. 1980;12(5-6):757-760.
http://dx.doi.org/10.1016/0020-711X(80)90158-5