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Lactose metabolism was studied in primary rabbit kidney cell culture. The differentiated epithelial cells cultured on a permeable membrane took up lactose (0.5-20 mmol/L) from the extracellular fluid; the rate of lactose uptake was maximal at 5-10 mmol/L and was linear for 1 hour. This lactose uptake was time- and concentration-dependent. Lactose uptake was saturated at the concentration of 20 mmol/L and was associated with cellular metabolism. Sulfhydryl reagents (N-ethylmaleimide, N-bromoacetamide) almost completely inhibited lactose uptake and metabolism. The product of lactose metabolism was lactate (0.5-10 mmol/L); when the extracellular lactose concentration was reduced below 10 mmol/L, the appearance of lactate was paralleled by a transient increase in intracellular glucose (5-20 mmol/L). Lactose and lactate could be recycled by the cells and the effect was equivalent to a transient addition of lactose. In cultures incubated in the presence of 13C-labeled lactose, lactose was incorporated into glycogen, which was labeled more heavily than cellular protein. After extraction of glycogen, 13C enrichment of protein was 21 times lower than that of glycogen. Fructose-1,6-bisphosphatase was responsible for this difference. This enzyme was partially inactivated by 0.05 mmol/L thiamin pyrophosphate. In contrast, no 13C enrichment of nucleotides
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