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Nonenzymatic Glucosylation Of Rat Albumin: Studies In Vitro And In Vivo, James F. Day, Robert W. Thornburg, Suzanne R. Thorpe, John W. Baynes
Nonenzymatic Glucosylation Of Rat Albumin: Studies In Vitro And In Vivo, James F. Day, Robert W. Thornburg, Suzanne R. Thorpe, John W. Baynes
Faculty Publications
Incubation of rat serum with D-glucose in vitro resulted in nonenzymatic glucosylation of serum proteins. Analysis of freshly isolated rat albumin by ion exchange chromatography indicated that the glucosylated albumin accounts for 6.7.+-. 0.9% of total albumin in normal rat serum. Glucosylation of rat albumin in vitro was 1st order with respect to glucose and albumin concentrations and occurs primarily (> 90%) at intrachain lysine residues. Kinetic analysis and inhibition of glucosylation by aspirin suggest that 1 reactive lysine residue is the primary site of glucosylation. Less than 5% of the radioactivity from glucosyl-albumin was released as glucose or mannose …
Nonenzymatically Glucosylated Albumin: In Vitro Preparation And Isolation From Normal Human Serum, James F. Day, Suzanne R. Thorpe, John W. Baynes
Nonenzymatically Glucosylated Albumin: In Vitro Preparation And Isolation From Normal Human Serum, James F. Day, Suzanne R. Thorpe, John W. Baynes
Faculty Publications
Incubation of human serum with D-[6-3H]glucose resulted in the gradual accumulation of radioactivity in acid-precipitable material. Upon chromatography on Sephadex G-200, radioactivity was found associated with each of the major molecular weight classes of serum protein. Purified human serum albumin was also glucosylated in vitro upon exposure to D-[6-3H]glucose in phosphate-buffered saline. The glucosylated and unmodified albumins were separated by ion exchange chromatography. The physiological significance of these observations in vitro was confirmed by the isolation and quantitation of glucosylated albumin from normal human serum. Glucosylated albumin represents approximately 6 to 15% of total serum albumin in normal adults. The …