| | 1 | Author
| Remigius Manderscheid, Aloysius Wild | Requires cookie* | | | Title
| Characterization of Glutamine Synthetase of Roots, Etiolated Cotyledons and Green Leaves from Sinapis alba (L.)  | | | | Abstract
| Glutamine synthetase of roots, etiolated cotyledons and green leaves from mustard plants cannot all clearly be separated by DEAE-Sephacel chromatography. However, the enzyme of the roots, etiolated cotyledons and green leaves, respectively, differed in the kinetic properties deter mined in the crude extract. The root enzyme showed a pH-optimum of about 6.9, a K m value of 3 m M for glutamate and a temperature optimum at 48 °C. Glutamine synthetase of etiolated cotyledons possessed a Km for glutamate of 6 or 12 m M , depending on the dithioerythritol con centration in the homogenisation buffer and a temperature optimum at 46 °C. The enzyme of green leaves was characterized by a temperature optimum at 40 °C, a pH-optimum at about 7.4 and a low glutamate affinity with positive cooperative substrate binding. Based on isolation of chloroplasts and identification of glutamine synthetase the enzyme of green leaves seems to be the chloroplastic form. This enzyme was purified by DEAE-Sephacel, hydroxylapatite and Sephacryl S-300 chromatography. Affinity for glutamate and M g S04 of the purified enzyme differed from that found in the crude extract. The function of the different isoenzymes is discussed. Intro du ction | | | |
Reference
| Z. Naturforsch. 41c, 712 (1986); received March 17 1986 | | | |
Published
| 1986 | | | |
Keywords
| Enzyme Purification, Glutamine Synthetase, Isoenzymes, Photorespiration, Sinapis alba | | | |
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| default:Reihe_C/41/ZNC-1986-41c-0712.pdf | | | | Identifier
| ZNC-1986-41c-0712 | | | | Volume
| 41 | |
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