Purification and characterization of creatine kinase, an estrogen-induced uterine protein (IP) from immature rats.

An estrogen-responsive translational product, the induced protein (IP) first described by Notides and Gorski (8), was obtained solely from the target organ, immature rat uterus, and purified to homogeneity in a procedure using two chromatography steps. The purified IP has a molecular weight of 49,000, and the isoelectric point is 5.2. Creatine kinase activity is associated with the homogeneous IP. There are some differences between the uterine enzyme and the creatine kinase BB isoenzyme, including differences in stability, and sensitivity to mercaptans. Estrogen-induced creatine kinase purified by this simple, reproducible method is a useful antigen for further studies on the translation and transcription processes involved in hormone-modulated synthesis.