Enzymatic characteristics of the guanylate cyclase of KB cells: their change as a function of the development of the cultures]

We have localized 71% of the guanylate cyclase activity in the (G X 105,000) supernatent fraction of broken KB cells. The reaction follows Michaelis-Menten kinetics, the apparent Km for GTP is 0,5 mM, as long as GTP is lower than a limited concentration, then activity is inhibited. The ion Mn++ is an absolutely required activator, it does not change enzyme-substrate affinity. The enzyme shows several types of binding sites of Mn++. Guanylate cyclase, studied over a period of development of culture, shows, in KB cells without cell contact, an activity higher than that observed in confluent cells. This is not due to the fact of a change in enzyme-substrate affinity but to a modification of Mn++ influence.     

The effect of oxine-5-sulphonic acid on the hepatic drug metabolism in the rat

Summary Oxine-5-sulphonic acid inhibits the metabolism of aminopyrine in the rat liver in vitro. The characteristics of this inhibition vary according to whether the oxidativeN-demethylation of the substrate is determined by the formation of the metabolite 4-aminoantipyrine or by the production of formaldehyde.     

A simple method for cultivating the early chick embryo in vitro

Summary A method for cultivating the early chick embryo in an artificial medium has been developed that permits the determination of the stage at the onset of the treatment and the continuous observation of the embryogenesis.Kungliga Fysiografiska Sällskapet, Lund, supported this work.