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Abstract:

1. 1. A method for purifying human erythrocytes ALA-D, using a mixture of n-butanol and chloroform, which denature hemoglobin, followed by ammonium sulphate fractionation and affinity chromatography yielding a 1600-fold purified enzyme, is described. 2. 2. By oxidation of Sephadex G-25 with NaIO4, a polyaldehyde, is obtained which can be covalently bound to the ALA-D; however the immobilized enzyme is inactive, because essential ε{lunate}-amino groups at the active site were involved in the coupling. Similar experiments with another enzyme, Rhodanese, resulted in an active insolubilized preparation. 3. 3. By suspending the carrier-enzyme in buffer, slow solubilization with simultaneous release of protein occurs, indicating that this approach might find important therapeutical applications in the treatment of enzyme deficiencies. © 1980.

Registro:

Documento: Artículo
Título:Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
Autor:Bustos, N.; Stella, A.M.; Xifra, E.A.W.D.; C. Batlle, A.M.D.
Filiación:Centro de Investigaciones Sobre Porfirinas y Porfirias (CIPYP), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires y Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET), Ciudad Universitaria, Pabellón II, 4 Piso Nuñez 1428, Buenos Aires, Argentina
Palabras clave:butanol; chloroform; porphobilinogen synthase; blood and hemopoietic system; enzyme purification; erythrocyte; human cell; in vitro study; normal human; preliminary communication; Enzymes, Immobilized; Erythrocytes; Human; Porphobilinogen Synthase; Support, Non-U.S. Gov't; Thiosulfate Sulfurtransferase
Año:1980
Volumen:12
Número:5-6
Página de inicio:745
Página de fin:749
DOI: http://dx.doi.org/10.1016/0020-711X(80)90156-1
Título revista:International Journal of Biochemistry
Título revista abreviado:Int. J. Biochem.
ISSN:0020711X
CODEN:IJBOB
CAS:butanol, 35296-72-1, 71-36-3; chloroform, 67-66-3; porphobilinogen synthase, 9036-37-7; Enzymes, Immobilized; Porphobilinogen Synthase, EC 4.2.1.24; Thiosulfate Sulfurtransferase, EC 2.8.1.1
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Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p745_Bustos

Referencias:

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  • Del Batlle, Ferramola, Grinstein, Purification and general properties of Delta Aminolaevulic Acid Dehydratase from cow liver (1967) Biochem. J., 104, pp. 244-249
  • Bonsignore, Delta Aminolaevulinate dehydratase activity of erythrocytes as a diagnostic test in occupational lead poisoning (1966) Med. Lavoro, 57, pp. 647-655
  • Chang, Methods for the therapeutic applications of immobilized enzymes (1976) Methods in Enzymology, 44, pp. 676-698. , K. Mosbach, Academic Press, London
  • Corcoran, Page, A method for the determination of mannitol in plasma and urine (1947) J. biol. Chem., 170, p. 165
  • Doss, Tieperman, Schneider, Schmid, Acute hepatic porphyria syndrome with porphobilinogen synthase defect (1979) Int. J. Biochem., 12, pp. 823-826
  • Gregoriadis, Buckland, Enzymecontaining liposomes alleviate a model for storage disease (1973) Nature, Lond., 244, pp. 170-172
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  • Hano, Akashi, Influences of anticancer agents on the metabolism of delta-aminolevulinic acid in normal and tumor bearing mice (1964) Gann., 55, pp. 25-30
  • Heilmeyer, Neue Ergebnisse der Porphyrinstoffwechselforschung (1963) Münch. med. Wschr., 105, pp. 277-287
  • Ivanov, Die Rolle der Delta-Aminolavulinsaure-Dehydrase (ALA-D) in der Erythrocyten bei der Erforschung der Biosynthese der Porphyrine (1968) Folia Haemat., 89, pp. 233-240
  • Lowry, Rossebrouoh, Farr, Randall, Protein measurement with the Folin-Phenol reagent (1951) J. biol. Chem., 193, pp. 265-275
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  • Polo, Stafforini, Stella, Wider, Del Batlle, (1980) Pig liver aminolevulinate dehydratase I. Alternative methods for its purification and properties of the enzyme, , In preparation
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  • Rubino, Teso, Rasetti, Erythrocyte delta-aminolaevulinic acid dehydratase in anemia (1960) Ada Haemal., 24, p. 300
  • Scott, Purification of red cell enzymes by treatment with n-butanol and chloroform (1976) Prep. Biochem., 6, pp. 147-152
  • Stella, Del Batlle, Porphyrin biosynthesis. Immobilized enzymes and ligands V. Purification of aminolevulinate dehydratase from bovine liver by affinity chromatography (1977) Int. J. Biochem., 8, pp. 353-358
  • Stella, Del Batlle, Porphyrin biosynthesis Immobilized enzymes and ligands VIII Studies on the purification of aminolevulinate dehydratase from Euglena gracilis (1978) Plant Science Letters, 2 (2), pp. 87-92
  • Stella, Wider, Del Batlle, Porphyrin biosynthesis. Immobilized enzymes and ligands IV. Studies on delta aminolevulinate dehydratase attached to Sepharose (1977) Mol. Cell. Biochem., 16, pp. 97-104
  • Wider, Sandy, Davies, Neubkrger, Control of 5-aminolevulinate synthetase activity in Rh spherondes (1976) Philosophical Transactions of the Royal Society B: Biological Sciences, 273, pp. 79-98

Citas:

---------- APA ----------
Bustos, N., Stella, A.M., Xifra, E.A.W.D. & C. Batlle, A.M.D. (1980) . Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications. International Journal of Biochemistry, 12(5-6), 745-749.
http://dx.doi.org/10.1016/0020-711X(80)90156-1
---------- CHICAGO ----------
Bustos, N., Stella, A.M., Xifra, E.A.W.D., C. Batlle, A.M.D. "Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications" . International Journal of Biochemistry 12, no. 5-6 (1980) : 745-749.
http://dx.doi.org/10.1016/0020-711X(80)90156-1
---------- MLA ----------
Bustos, N., Stella, A.M., Xifra, E.A.W.D., C. Batlle, A.M.D. "Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications" . International Journal of Biochemistry, vol. 12, no. 5-6, 1980, pp. 745-749.
http://dx.doi.org/10.1016/0020-711X(80)90156-1
---------- VANCOUVER ----------
Bustos, N., Stella, A.M., Xifra, E.A.W.D., C. Batlle, A.M.D. Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications. Int. J. Biochem. 1980;12(5-6):745-749.
http://dx.doi.org/10.1016/0020-711X(80)90156-1