Homology between a prolyl hydroxylase subunit and a tissue protein that crossreacts immunologically with the enzyme.

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Abstract
A protein, enzymatically inactive but immunologically related to prolyl hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase; EC 1.14.11.2) (cross-reacting protein), was purified to near homogeneity from skin of newborn rats. The purified protein has a MW of 60,000 on gel filtration and sodium dodecyl sulfate gel electrophoresis, corresponding to that of the smaller of the 2 dissimilar subunits of the enzyme. The 2 subunits of prolyl hydroxylase differ markedly from one another in their amino acid compositions, but cross-reacting protein and the smaller subunit are very similar in composition. On antibody-affinity chromatography both subunits reacted with the antibody developed against the inact enzyme. Neither cross-reacting protein nor the 60,000 MW subunit was absorbed onto concanavalin A, which absorbed the intact enzyme as well as the larger subunit. Crossreacting protein is apparently identical to 1 of the subunits of prolyl hydroxylase or metabolically related to it.

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