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Sancovich, H.A.; Ferramola, A.M.; Del Batlle, C.A.M. "Studies on cow liver porphobilinogen deaminase" (1976) Acta Physiologica Latino-Americana. 26(5):379-386
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Abstract:

Further properties of cow liver deaminase are reported. Highly purified deaminase migrated as a single band on starch and polyacrylamide gels electrophoresis. Molecular weight determinations by means of gel filtration on calibrated columns of Sephadex G-100, Sepharose 4 B and B10-Gel P-100 gave values of 40,000 ± 4,000. Data obtained suggest that cow liver deaminase exists as a single polypeptide chain. Heating partially purified preparations of deaminase resulted in an enhancement of activity. Added cosynthetase to these fractions increased the percentage of uroporphyrinogen III formed but also diminished total uroporphyrinogens synthesis. The action of several compounds added to the system was studied. Thiol reagents and divalent metals as Hg2+, Pb2+, Cd2+ inhibited deaminase, indicating the presence of thiol groups essential for activity, probably involved in the cyclization step. Certain concentrations of sodium, potassium and magnesium salts enhanced activity. Several chelators tested were without effect on the deaminase. Some dicarboxylic acids and 2-methoxy-5-nitrotropone inhibited the enzyme.

Registro:

Documento: Artículo
Título:Studies on cow liver porphobilinogen deaminase
Autor:Sancovich, H.A.; Ferramola, A.M.; Del Batlle, C.A.M.
Filiación:Lab. Porfirinas, Dept. Quim. Biol., Fac. Ci. Exact. Naturales, Ciud. Univ., Buenos Aires, Argentina
Palabras clave:porphobilinogen deaminase; animal experiment; cattle; in vitro study; liver; Ammonia-Lyases; Animal; Cations, Divalent; Cattle; Chelating Agents; Electrophoresis, Polyacrylamide Gel; Electrophoresis, Starch Gel; Female; Heat; Hydroxymethylbilane Synthase; Liver; Molecular Weight; Sulfhydryl Reagents
Año:1976
Volumen:26
Número:5
Página de inicio:379
Página de fin:386
Título revista:Acta Physiologica Latino-Americana
Título revista abreviado:ACTA PHYSIOL. LAT.-AM.
CODEN:APLTA
CAS:porphobilinogen deaminase, 9036-47-9, 9074-91-3; Ammonia-Lyases, EC 4.3.1.; Cations, Divalent; Chelating Agents; Hydroxymethylbilane Synthase, EC 4.3.1.8; Sulfhydryl Reagents
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich

Citas:

---------- APA ----------
Sancovich, H.A., Ferramola, A.M. & Del Batlle, C.A.M. (1976) . Studies on cow liver porphobilinogen deaminase. Acta Physiologica Latino-Americana, 26(5), 379-386.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich [ ]
---------- CHICAGO ----------
Sancovich, H.A., Ferramola, A.M., Del Batlle, C.A.M. "Studies on cow liver porphobilinogen deaminase" . Acta Physiologica Latino-Americana 26, no. 5 (1976) : 379-386.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich [ ]
---------- MLA ----------
Sancovich, H.A., Ferramola, A.M., Del Batlle, C.A.M. "Studies on cow liver porphobilinogen deaminase" . Acta Physiologica Latino-Americana, vol. 26, no. 5, 1976, pp. 379-386.
Recuperado de https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich [ ]
---------- VANCOUVER ----------
Sancovich, H.A., Ferramola, A.M., Del Batlle, C.A.M. Studies on cow liver porphobilinogen deaminase. ACTA PHYSIOL. LAT.-AM. 1976;26(5):379-386.
Available from: https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich [ ]