“…As the amount of soluble GGT in the cytosol of 1 A preliminary report of some of these findings was presented at the International Symposium Neuroontogeneticum Tertium, Prague, July 9-14, 1979. different animal cells is limited [6,25], the soluble activity of this enzyme in body fluids probably originates from cell membrane sur faces [12] where GGT is attached as an ectoenzyme. While the soluble enzyme in blood plasma is mainly of hepatic origin [1,12], its presence in CSF might reflect not only a rapid turnover of the membrane surfaces of lining ependymal cells and choroid plexus epitheli um [2,18,34] which have a high activity of GGT, but also of naturally occurring cell loss in the embryonic brain and spinal cord [8,27], Because of the lack of data concerning the developmental formation and cortisol regula tion of GGT in liver, choroid plexus, blood plasma and CSF of chick embryo, it seemed to be of interest to describe the development al profile of the membrane-bound and solu ble form of GGT in the embryonic organs and body fluids. This may then point to a possible relationship of the soluble form of the en zyme with that which is bound to cell mem branes of embryonic organs and tissues, and might also reveal a regulatory effect of corti sol on these two forms of GGT in the embry onic chick.…”