Studies on cow liver porphobilinogen deaminase
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 valu...
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| Otros Autores: | , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
1976
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| Acceso en línea: | Registro en Scopus Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| LEADER | 03234caa a22005177a 4500 | ||
|---|---|---|---|
| 001 | PAPER-18664 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205002.0 | ||
| 008 | 190411s1976 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0017051959 | |
| 024 | 7 | |2 cas |a 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 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a APLTA | ||
| 100 | 1 | |a Sancovich, H.A. | |
| 245 | 1 | 0 | |a Studies on cow liver porphobilinogen deaminase |
| 260 | |c 1976 | ||
| 506 | |2 openaire |e Política editorial | ||
| 520 | 3 | |a 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. |l eng | |
| 593 | |a Lab. Porfirinas, Dept. Quim. Biol., Fac. Ci. Exact. Naturales, Ciud. Univ., Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a PORPHOBILINOGEN DEAMINASE |
| 690 | 1 | 0 | |a ANIMAL EXPERIMENT |
| 690 | 1 | 0 | |a CATTLE |
| 690 | 1 | 0 | |a IN VITRO STUDY |
| 690 | 1 | 0 | |a LIVER |
| 690 | 1 | 0 | |a AMMONIA-LYASES |
| 690 | 1 | 0 | |a ANIMAL |
| 690 | 1 | 0 | |a CATIONS, DIVALENT |
| 690 | 1 | 0 | |a CATTLE |
| 690 | 1 | 0 | |a CHELATING AGENTS |
| 690 | 1 | 0 | |a ELECTROPHORESIS, POLYACRYLAMIDE GEL |
| 690 | 1 | 0 | |a ELECTROPHORESIS, STARCH GEL |
| 690 | 1 | 0 | |a FEMALE |
| 690 | 1 | 0 | |a HEAT |
| 690 | 1 | 0 | |a HYDROXYMETHYLBILANE SYNTHASE |
| 690 | 1 | 0 | |a LIVER |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a SULFHYDRYL REAGENTS |
| 700 | 1 | |a Ferramola, A.M. | |
| 700 | 1 | |a Del Batlle, C.A.M. | |
| 773 | 0 | |d 1976 |g v. 26 |h pp. 379-386 |k n. 5 |p ACTA PHYSIOL. LAT.-AM. |t Acta Physiologica Latino-Americana | |
| 856 | 4 | 1 | |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017051959&partnerID=40&md5=679a49c949801ccc466e6896032366bb |y Registro en Scopus |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_NIS18664_v26_n5_p379_Sancovich |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18664_v26_n5_p379_Sancovich |y Registro en la Biblioteca Digital |
| 961 | |a paper_NIS18664_v26_n5_p379_Sancovich |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 999 | |c 79617 | ||