The phosphorylated carbohydrate intermediates of erythrocytes from normal adults and from five patients with hereditary spherocytosis (HS) were labeled in vitro with P32 orthophosphate and then separated on columns of ion exchange resin.

No qualitative or quantitative differences were found between normal and HS erythrocytes.

The relative specific activity of each phosphate of 2, 3 DPG was the same; whereas the phosphate attached to ribose in ADP and ATP was not labeled. The nucleotides were labeled at a much faster rate than DPG. When the erythrocytes were washed 6 or more times, the specific activity of Pi approached that of DPG. No definite difference was found in the rate of labeling of the intermediates from normal and HS erythrocytes.

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