Glyoxalase I and glyoxalase II from Aloe vera: purification, characterization and comparison with animal glyoxalases.
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.
Norton
S J
SJ
Department of Biochemistry, University of North Texas, Denton.
Talesa
V
V
Yuan
W J
WJ
Principato
G B
GB
D000504:Aloe / Q000201:enzymology*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D007700:Kinetics; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D010946:Plants, Medicinal; D013045:Species Specificity; D013869:Thiolester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000099301:Hydroxyacylglutathione Hydrolase
D007791:Lactoylglutathione Lyase; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase