Immunological Studies on CTP:Phosphocholine Cytidylyltransferase from the Livers of Normal and Choline‐Deficient Rats

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Abstract
Chickens were immunized with the purified low-MW form of CTP:phosphocholine cytidylyltransferase from rat liver cytosol. The antiserum was obtained and fractionated to yield immunoglobulin. The antibodies specifically inhibited the enzymatic activity of the partially prufied low-MW form of the enzyme from pH 6.0-8.5. Antibodies against the low-MW form of the enzyme cross-reacted with the high-MW form of the enzyme from cytosol and with the cytidylyltransferase associated with the microsomal fraction. The antibodies were used for the immunochemical determination of the amount of cytosolic phosphocholine cytidylyltransferase in the livers of normal and choline-deficient rats. The amount of enzyme in rat liver cytosol was not changed for at least 18 days of choline deficiency. The decrease in specific activity of the enzyme in choline-deficiency may be cuased caused by factors other than adaptive changes in the enzyme level.