Effects of 3-deoxyglucosone on the Maillard reaction.

We investigated the effect of exogenously applied 3-deoxyglucosone, a major carbonyl intermediate, on the Maillard reaction. The fluorescence intensity of the product of the reaction of bovine serum albumin with 3-deoxyglucosone was higher than that with an equivalent amount of glucose. Similarly the rate of polymerization of lysozyme in the presence of 3-deoxyglucosone was also greater than with glucose, and collagen incubated with 3-deoxyglucosone was less digestible than collagen incubated with glucose. By contrast, aminoguanidine inhibited an increase in fluorescence of the Maillard compounds and the polymerization of protein, both of which were stimulated by 3-deoxyglucosone. These results suggest that 3-deoxyglucosone accelerates the advanced stage of the Maillard reaction and that aminoguanidine acts on 3-deoxyglucosone to inhibit its action in the advanced stage of the Maillard reaction.

[1]  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.

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

[3]  M. Oimomi,et al.  Glycation of cataractous lens in non-diabetic senile subjects and in diabetic patients. , 1988, Experimental eye research.

[4]  F. G. NjorogeS,et al.  Mechanism of Formation of the Putative Advanced Glycosylation End , 1988 .

[5]  R. Cho,et al.  Responsibility of 3-Deoxyglucosone for the Glucose-Induced Polymerization of Proteins , 1987 .

[6]  A. Cerami,et al.  Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. , 1986, Science.

[7]  S. Pongor,et al.  Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[8]  V. Monnier,et al.  Collagen Aging In Vitro by Nonenzymatic Glycosylation and Browning , 1984, Diabetes.

[9]  A. Cerami,et al.  Excessive Nonenzymatic Glycosylation of Peripheral and Central Nervous System Myelin Components in Diabetic Rats , 1983, Diabetes.

[10]  V. Monnier,et al.  Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. , 1981, Science.

[11]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[12]  K. Weber,et al.  The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. , 1969, The Journal of biological chemistry.

[13]  S. Rahbar.  An abnormal hemoglobin in red cells of diabetics. , 1968, Clinica chimica acta; international journal of clinical chemistry.

[14]  F S LABELLA,et al.  STRUCTURE OF COLLAGEN FROM HUMAN TENDON AS INFLUENCED BY AGE AND SEX. , 1965, Journal of gerontology.

[15]  H. Kato.  Chemical Studies on Amino––Carbonyl Reaction , 1962 .