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- W2068875716 abstract "The lability of lactose biosynthesis in bovine mammary cell cultures contrasts with the more prolonged synthesis of β-lactoglobulin. Studies on cellular products and associated enzymatic pathways indicated that UDPG pyrophosphorylase activity dropped rapidly with time corresponding to the loss in lactose synthesis but then leveled off at an activity corresponding to the synthesis of glycogen. The main carbohydrate synthesized with time became glycogen instead of lactose and the bulk of glucose not utilized in this manner was shunted into protein and nucleic acid synthesis. Insulin enhanced this occurrence. With galactose provided as the major hexose and some glucose present, the continuation of lactose synthesis as well as the conversion of galactose to glucose was enhanced thus maintaining both the activities of UDPGal-4-epimerase and galactosyl transferase. Indications were found that other conditions such as low serum level, increased defined medium constituents (particularly glucose), and increased cell density may also be factors in maintaining lactose synthesis." @default.
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- W2068875716 date "1964-03-01" @default.
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- W2068875716 title "Induced enzymatic changes in lactose synthesis and associated pathways of bovine mammary cell cultures" @default.
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- W2068875716 doi "https://doi.org/10.1016/0014-4827(64)90185-5" @default.
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