On the Physiological Significance of the Isoenzyme Groups of Peroxidase from Tabacco Demonstrated by Biochemical Properties I. Separation, Purification, Chemical and Physical Properties
| dc.contributor.author | Nessel, A. | |
| dc.contributor.author | Mader, M. | |
| dc.date.accessioned | 2014-09-09T09:14:18Z | |
| dc.date.available | 2014-09-09T09:14:18Z | |
| dc.date.issued | 1977 | |
| dc.description.abstract | Separation and purification of three peroxidase-isoenzyme groups (GI, fast migrating anodic; GH, slow migrating anodic; GIII, slow migrating cathodic) was accomplished by ion-exchange chromatography. Chromatographic separation of the groups was controlled by disk-electrophoresis and by isoelectric focusing. Molecular weights were estimated by SDS-gelelectrophoresis and by thin layer chromatography. The results of both methods are similar. GI has a molecular weight of about 27,000, GH of 43,000 and GIII of 47,000. By affinity chromatography with Coocanavalin A-sepharose it was shown that the enzymes of the three peroxidase groups are all glycoproteins. While heat inactivation of GI was measured at 50 °C, inactivation of GII and GIII did not take place before 70 °C. Absorption spectra of the three groups were typical for ferriperoxidases with the maximum of the Soret band at 401 nm. | en_US |
| dc.identifier.citation | Z.Pflanzenphysiol.Bd.82.S, 235-246, 1977 | en_US |
| dc.identifier.uri | http://hdl.handle.net/123456789/5532 | |
| dc.language.iso | en | en_US |
| dc.subject | peroxidase | en_US |
| dc.subject | izoenzymes | en_US |
| dc.subject | biochemical characterization | en_US |
| dc.subject | callus cultures | en_US |
| dc.subject | nicotiana tabacum | en_US |
| dc.title | On the Physiological Significance of the Isoenzyme Groups of Peroxidase from Tabacco Demonstrated by Biochemical Properties I. Separation, Purification, Chemical and Physical Properties | en_US |
| dc.type | Article | en_US |