Matrix-assisted laser desorption/ionization mass spectrometric studies on protein glycation. 2. The reaction of ribonuclease with hexoses†

The products arising from the reactions of ribonuclease with glucose or fructose have been studied by means of matrix-assisted laser desorption/ionization mass spectrometry. The reactions have been carried out at physiological pH, with two different sugar concentrations and different incubation times. A maximum increase in molecular weight, corresponding to 485 Da, was found in the case of ribonuclease incubated with 0.25 M fructose for 6 days. Furthermore clear differences have been found in the reactivity of glucose and fructose; in particular, while glucose reacts faster than fructose in the early stage of the glycation, the rearrangements of the Amadori adducts are favoured using fructose as reagent sugar.

[1]  C. Gerhardinger,et al.  A study on in vitro glycation processes by matrix-assisted laser desorption ionization mass spectrometry. , 1993, Biochimica et biophysica acta.

[2]  N. Taniguchi,et al.  Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species. , 1992, The Journal of biological chemistry.

[3]  H. Halsall,et al.  Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein. , 1992, The Biochemical journal.

[4]  J. Henion,et al.  Structural characterization of protein tryptic peptides via liquid chromatography/mass spectrometry and collision-induced dissociation of their doubly charged molecular ions. , 1991, Analytical chemistry.

[5]  J. Baynes,et al.  Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. , 1991, The Journal of biological chemistry.

[6]  V. Monnier,et al.  Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. , 1991, The Journal of biological chemistry.

[7]  J. Peter-Katalinic,et al.  The use of fast atom bombardment and laser desorption mass spectrometry in the analysis of complex carbohydrates , 1991 .

[8]  C. Gerhardinger,et al.  Evidence of acid hydrolysis as responsible for 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole (FFI) production. , 1990, Clinica chimica acta; international journal of clinical chemistry.

[9]  V. Monnier,et al.  Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. , 1989, The Journal of biological chemistry.

[10]  A. Oronsky,et al.  Nonenzymatic glycation of bovine serum albumin by fructose (fructation). Comparison with the Maillard reaction initiated by glucose. , 1989, The Journal of biological chemistry.

[11]  V. Monnier,et al.  Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-1H-imidazole. , 1988, The Journal of biological chemistry.

[12]  B. Shilton,et al.  Role of fructose in glycation and cross-linking of proteins. , 1988, Biochemistry.

[13]  J. Baynes,et al.  Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. , 1986, The Journal of biological chemistry.

[14]  F. Hayase,et al.  Maillard Reaction Products from D-Glucose and Butylamine , 1985 .

[15]  A. Cerami,et al.  Nonenzymatic glycosylation and the pathogenesis of diabetic complications. , 1984, Annals of internal medicine.

[16]  L.,et al.  Glucosylation of human collagen in aging and diabetes mellitus. , 1980, The Journal of clinical investigation.

[17]  K. Gabbay,et al.  Hyperglycemia, polyol metabolism, and complications of diabetes mellitus. , 1975, Annual review of medicine.

[18]  J. Tatum,et al.  Degradation of d-glucose with acetic acid and methylamine☆ , 1970 .

[19]  T. Reynolds.  Chemistry of nonenzymic browning. II. , 1965, Advances in food research.