Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases - PubMed (original) (raw)
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- PMID: 2076100
Comparative Study
Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases
S J Norton et al. Biochem Int. 1990 Nov.
Abstract
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.
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