Bovine liver porphobilinogenase (PBGase) has been covalently attached to Sepharose, and some of their properties have been studied. The optimal conditions for binding have been determined. The water-insoluble PBGase retained a high percentage of the activity of the soluble enzyme; the coupling yield was also high. Sepharose-PBGase could be stored at 4°C for periods up to 5 weeks with 40% loss of activity and it could be repeatedly used with little alteration of its enzymic activity; however, both by storage and repeated use, isomerase was inactivated and the percentage of uroporphyrinogen I formed was increased. Attachment of PBGase to Sepharose has led to enhanced thermal stability. pH optima of the insolubilized enzyme was shifted 0.6 units towards the alkaline side as compared to that of the native enzyme.
| Documento: | Artículo |
| Título: | Porphyrin biosynthesis. Immobilized enzymes and ligands. VII. Studies on bovine liver porphobilinogenase |
| Autor: | Rossetti, M.V.; Parera, V.E.; Del Batlle, C.A.M. |
| Filiación: | Lab. de Porfirinas, Dept. Quim. Biol., Fac. Ci. Exact. Naturales, Ciud. Univ., Buenos Aires, Argentina |
| Palabras clave: | enzyme; porphyrin; animal experiment; cattle; in vitro study; liver; porphobilinogenase; Ammonia-Lyases; Animal; Cattle; Enzymes, Immobilized; Hydrogen-Ion Concentration; Ligands; Liver; Porphyrins; Protein Binding; Sepharose; Temperature |
| Año: | 1976 |
| Volumen: | 26 |
| Número: | 5 |
| Página de inicio: | 371 |
| Página de fin: | 378 |
| Título revista: | Acta Physiologica Latino-Americana |
| Título revista abreviado: | ACTA PHYSIOL. LAT.-AM. |
| CODEN: | APLTA |
| CAS: | porphyrin, 24869-67-8; Ammonia-Lyases, EC 4.3.1.; Enzymes, Immobilized; Ligands; Porphyrins; Sepharose, 9012-36-6 |
| Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_NIS18665_v26_n5_p371_Rossetti |
