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J. Biol. Chem., Vol. 261, Issue 31, 14557-14561, 11, 1986
CM Gundberg, M Anderson, I Dickson and PM Gallop
Purified osteocalcin from cow and calf bone was analyzed for nonenzymatic
glycosylation (glycation) by sodium [3H]borohydride reduction. Calf bone
was found to be approximately 5% glycated, while bone from mature cows was
10% glycated. These results were confirmed by a second method which
utilizes periodate oxidation followed by formaldehyde fluorescence.
Osteocalcin in human bone was also found to be glycated. The content of
glycated osteocalcin from the bones of 47 nondiabetic individuals, aged
0.6-97, was dependent upon age. The extent of glycation was lowest in
children, was constant through the adult years, and increased linearly in
bone taken from individuals aged 60-97. Glycated osteocalcin was purified
by boronate affinity chromatography and subjected to one-step Edman
degradation. It was established that the site of glycation was the
amino-terminal tyrosine. Increases in the amount of glycated osteocalcin in
the bones of older individuals may play a role in the pathogenesis of
senile osteoporosis and in the osteopenia which may accompany diabetes
mellitus.
"Glycated" osteocalcin in human and bovine bone. The effect of age
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