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- W2078357346 abstract "In 3T6 mouse fibroblast cultures, ascorbate has two separate roles in the hydroxylation of collagen proline. In one of these, its co-factor role in vitro, it can be replaced by a variety of reducing agents, notably low molecular weight thiol compounds; the latter however also cause irreversible inactivation of the enzyme. In its second role, ascorbate appears to act in the same manner as high lactate concentration and high cell density: by catalysing the formation of active enzyme inside the cell. Reduction in oxygen tension, an uncoupling agent and several other circumstances, can also produce this effect. The in vivo activation effect seems to be largely responsible for the stimulation of proline hydroxylation by ascorbate in growing cultures." @default.
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- W2078357346 date "1974-01-25" @default.
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- W2078357346 title "The activation of protocollagen proline hydroxylase by ascorbic acid in cultured 3T6 fibroblasts" @default.
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