Effects of female hormones on the activity of 3'-phosphoadenylylsulphate: desulphated heparan sulphate sulphotransferase in the endometrium of rabbit uterus.

Sulphotransferase activity in the microsomal fraction of the uterine endometrium of rabbits was measured with heparan sulphate, N-desulphated heparan sulphate and N-, O-desulphated heparan sulphate as exogenous substrates in the presence of 3'-phosphoadenylyl[35S]sulphate. Of the three acceptors, N-, O-desulphated heparan sulphate was most effectively radiolabelled. When N-, O-desulphated heparan sulphate was used as an acceptor, it was found that estrogen enhanced the sulphotransferase activity and that progesterone suppressed the effect of estrogen.