The turnover of F-actin-bound ADP in vivo.

A procedure for estimating the rate of turnover of F-actin-bound ADP in vivo is described. A turnover rate of 0.88 h-1 was determined for mouse muscle F-actin. The validity of the method when used to estimate the turnover rate of F-actin per se is discussed in relation to the possible exchange of F-actin-bound ADP.     

Serum prolactin levels and maintenance of progeny by prenatally-stressed female offspring.

Prenatal stress significantly reduced the number of progeny born to 47% of the female offspring and significantly increased the incidence of low birthweight young. None of these litters survived by the tenth postpartum day when serum prolactin levels were significantly reduced. Upon autopsy, these females had twice as many uterine implantation sites than the number of fetuses they bore, suggesting that a) the reduced postpartum serum prolactin most likely was the cause rather than the effect of the neonatal mortality and b) major hormonal deficiencies (possibly gonadotropic-related) were present even before giving birth.     

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.