Open AccessImmunological Studies on CTP:Phosphocholine Cytidylyltransferase from the Livers of Normal and Choline‐Deficient Rats
Author(s) -
CHOY Patrick C.,
SCHNEIDER Wolfgang Johann,
VANCE Dennis E.
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12227.x
Subject(s) - phosphocholine , choline , cytosol , enzyme , phosphorylcholine , biochemistry , antiserum , antibody , chemistry , microsome , enzyme assay , microbiology and biotechnology , biology , phospholipid , phosphatidylcholine , immunology , membrane
Chickens were immunized with the purified low‐molecular‐weight 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 purified low‐molecular‐weight form of the enzyme from pH 6.0 to 8.5. Antibodies against the low‐molecular‐weight form of the enzyme cross‐related with the high‐molecular‐weight form of the enzyme from cytosol as well as 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 caused by factors other than adaptive changes in the level of enzymes.