Purification and characterization of a membrane-bound deglycating enzyme (1-deoxyfructosyl alkyl amino acid oxidase, EC 1.5.3) from a Pseudomonas sp. soil strain.

The Journal of Biological Chemistry
A K SaxenaVincent M Monnier

Abstract

Searching for novel approaches for uncoupling glycation from hyperglycemia as a cause of diabetic complications, a Pseudomonas sp. soil strain containing a membrane-bound enzyme that deglycates amino acids under release of free fructosamine was isolated (Gerhardinger, C., Marion, S. M., Rovner, A., Glomb, M., and Monnier, V. M. (1995) J. Biol. Chem. 270, 218-224). This enzymatic activity was found to be very sensitive to inactivation by most detergents. From the plasma membrane ( approximately 3 mg/ml protein concentration), the enzyme could be solubilized in active form using 10 mM 3-[(3-chlolamidopropyl) dimethylammonio]-2-hydroxy-1-propanesulfonate aided by 2 M NaCl and 10% glycerol (27% optimal solubilization yield). The supernatant from a 55% saturation (NH4)2SO4 cut was fractionated onto a phenyl-Superose HR 5/5 column and enzymatic activity was eluted with a inverse gradient of (NH4)2SO4. Following removal of (NH4)2SO4 with PD-10 columns and fractionation with a Mono Q HR 5/5 column, a sharp peak of enzyme activity was eluted. Analysis on sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a major band at 106 kDa and, on isoelectrofocusing gel, a pI of 5.1. The activity was completely inhibited by CN- and ...Continue Reading

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