Nature of nonenzymatically bound hexose in hemoglobin, albumin, and crystallin.
Glucose incorporated in vitro during nonenzymatic glucosylation into albumin and hemoglobin was fully reducible by sodium borohydride unlike native albumin. Further, a prior hydrolysis under mild conditions (1 M oxalic acid:2 M HCl, 4 hr) was not required for in vitro incorporated glucose to yield maximal color intensity in the phenol-sulfuric acid reaction. Glucosyl-albumin, glucosyl-crystallin, and hemoglobin A1 behaved similarly in this respect. Hexose bound to HbA0 which alone showed an enhanced color intensity on prior acid hydrolysis was also not easily reduced by sodium borohydride. L-Cysteine (0.023 M) enhanced the color yield of glucosyl-hemoglobin, glucosyl-albumin, and glucosyl-crystallin to a lesser extent compared to fructose in the phenol-sulfuric acid reaction. Urea (6 M) also marginally increased the color intensity of glucosyl proteins and fructose.
D001894:Borohydrides; D003459:Crystallins / Q000032:analysis*; D005947:Glucose / Q000032:analysis; D006442:Glycated Hemoglobin / Q000031:analogs & derivatives* / Q000032:analysis; D006601:Hexoses / Q000032:analysis*; D006801:Humans; D010084:Oxidation-Reduction; D011485:Protein Binding; D012709:Serum Albumin / Q000032:analysis*
D001894:Borohydrides; D003459:Crystallins; D005947:Glucose; D006442:Glycated Hemoglobin; D006601:Hexoses; D012709:Serum Albumin; C025617:glucosylated hemoglobin A; C025616:glucosylated serum albumin; C025364:sodium borohydride