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 mHCl, 4 hr) was not required for in vitro incorporated glucose to yield ma...
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Published in | Biochemical medicine Vol. 34; no. 1; pp. 112 - 119 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
01.08.1985
Academic Press |
Subjects | |
Online Access | Get full text |
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Summary: | 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
mHCl, 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 A
1 behaved similarly in this respect. Hexose bound to HbA
0 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-2944 1557-7996 |
DOI: | 10.1016/0006-2944(85)90068-7 |