Abstract

Vitamin K-dependent carboxylation of protein has been obtained in microsomes from K-deficient rats by supplementing the microsomes with either a reduced pyridine nucleotide or dithiothreitol. γ-Carboxyglutamate residues have been directly identified as the radioactive reaction product after incubating the microsomes with NaH 14CO 3 and vitamin K. Evidence is presented that vitamin K is reduced to the hydroquinone prior to its involvement in carboxylation and that dithiothreitol has an additional role of protecting a critical sulfhydryl group. A structure-activity study using a variety of vitamins K and related compounds is reported.

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