title: Alloxan-diabetes alters kinetic properties of the membrane-bound form, but not of the soluble form, of acetylcholinesterase in rat brain.
abstract: We examined the effects of alloxan-diabetes on the kinetic properties of the soluble and the membrane-bound forms of acetylcholinesterase (AChE) in rat brain. The Km (0.15 mM) and Vmax. (1.5 mmol/min per mg of protein) of the soluble form of the enzyme were unchanged in the diabetic animals. The membrane-bound enzyme in the control group displayed a lower Km (0.09 mM) and a higher Vmax. (7.2 mmol/min per mg of protein) compared with the soluble form of the enzyme; the diabetic state caused a significant increase (40%) in both Km and Vmax. Kis values were about 3-4 times higher for the membrane-bound enzyme in both control and diabetic animals. The results suggest that membrane binding and membrane alterations in diabetes can significantly influence the kinetic properties of AChE.
authors.affiliation: Department of Biochemistry, Faculty of Science, M.S. University of Baroda, India.
authors.forename: M A
authors.initials: MA
authors.lastname: Khandkar
authors.forename: E
authors.initials: E
authors.lastname: Mukherjee
authors.forename: D V
authors.initials: DV
authors.lastname: Parmar
authors.forename: S S
authors.initials: SS
authors.lastname: Katyare
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D001835:Body Weight / Q000502:physiology; D001921:Brain / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D007700:Kinetics; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
chemical_list: D008565:Membrane Proteins; D000110:Acetylcholinesterase