Abstract
1. 1. Prolyl hydroxylase activity extracted from regenerating newt ( Notophthalmus viridescens) limb tissues can be increased by brief preincubation with cofactors (ascorbate, α-ketoglutarate, Fe 2+ and O 2) prior to assay with [ 3H]proline-labeled collagen substrate. 2. 2. Newt prolyl hydroxylase is optimally active at 30°C, but loses activity rapidly at 37°C. The presence of cofactors or substrate decreases enzyme heat lability. 3. 3. Detergents (Triton X-100 and octyl glucoside) do not aid enzyme extraction and inhibit enzyme activity. Activity solubilized during homogenization without detergent remains soluble following high speed centrifugations. 4. 4. Comparative studies are reported for enzyme extracted from chick embryo tissues.
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