Glyoxalase I and glyoxalase II from the outer green rind of Aloe vera leaves were purified by (matrix) affinity ligand-enzyme binding methods. The purified enzymes exhibited single protein bands on SDS-PAGE electrophoresis, with MW values of approximately 44,000 and 27,000 for glyoxalase I and glyoxalase II, respectively. The glyoxalase I is a basic protein (pI 7.8), while the glyoxalase II (3 protein bands) is acidic (pI 4.7, 4.8 [prevalent form], and 5.0). The kinetic constants, Km and Vmax, and Ki values for certain inhibitors are reported for both glyoxalase I and glyoxalase II. The glyoxalase enzymes from Aloe vera were compared with reported animal and plant glyoxalases.
Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases. / Norton SJ.; Talesa V.; Yuan WJ.; Principato GB.. - In: BIOCHEMISTRY INTERNATIONAL. - ISSN 0158-5231. - 22/1990:3(1990), pp. 411-418.
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Titolo: | Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases. |
Autori: | |
Data di pubblicazione: | 1990 |
Rivista: | |
Citazione: | Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases. / Norton SJ.; Talesa V.; Yuan WJ.; Principato GB.. - In: BIOCHEMISTRY INTERNATIONAL. - ISSN 0158-5231. - 22/1990:3(1990), pp. 411-418. |
Abstract: | Glyoxalase I and glyoxalase II from the outer green rind of Aloe vera leaves were purified by (ma...trix) affinity ligand-enzyme binding methods. The purified enzymes exhibited single protein bands on SDS-PAGE electrophoresis, with MW values of approximately 44,000 and 27,000 for glyoxalase I and glyoxalase II, respectively. The glyoxalase I is a basic protein (pI 7.8), while the glyoxalase II (3 protein bands) is acidic (pI 4.7, 4.8 [prevalent form], and 5.0). The kinetic constants, Km and Vmax, and Ki values for certain inhibitors are reported for both glyoxalase I and glyoxalase II. The glyoxalase enzymes from Aloe vera were compared with reported animal and plant glyoxalases. |
Handle: | http://hdl.handle.net/11391/920048 |
Appare nelle tipologie: | 1.1 Articolo in rivista |