Human plasma dopamine-β-hydroxylase: Oxygen and thermal stability

Summary There are wide individual variations in the thermal stability of human plasma dopamine--hydroxylase (DBH). Thermal stability variations have proven of value in biochemical genetic studies of many enzymes. The development of DBH thermolability depends on the exposure of plasma to oxygen. This observation may help to elucidate the biochemical basis of the genetic regulation of DBH.This work was supported in part by NIH grants HL 17487 and NS 11014.     

In vivo effects of Escherichia coli endotoxin on sulfobromophthalein clearance in the guinea-pig.

In vivo studies indicated that the primary effects of E. coli endotoxin on hepatic clearance of sulfobromophthalein were at the excretory level. Newborns were more sensitive to the LPS than older animals.     

Irreversible shock in rats after injection of microspheres into the renal artery

Summary After injection of microspheres into both renal arteries of rats, an irreversible shock syndrome develops, resulting in death within 4–12 h. Ligation of both renal pedicles after injection of microspheres prevents the shock. It is presumed that kininogenases released from the kidneys participate in the pathogenesis of the shock syndrome.These studies were supported in part by the Deutsche Forschungsgemeinschaft within the SFB 90, Cardiovasculäres System.     

Sensitivity of the developing chick myocardium to the positive inotropic effects of calcium and isoproterenol

Summary The present results show that the sensitivity of the chick myocardium to the positive motropic effect of Ca⁺⁺ decreases during development and that the Ca⁺⁺ concentration of the physiological solution used must be lowered below normal to study the effects of positive inotropic agents in preparations from younger embryos. Isoproterenol elicits positive inotropic responses in 7–9-day embryonic ventricle and in newborn chick atria; however, the 4-day embryonic myocardium is unresponsive to isoproterenol.This work was supported by Grant No. HL-15995 from the National Heart Institute (USPHS).The authors would like to thank Dr.F. E. Shideman for the isolated tissue baths used in these experiments.     

An electrophoretic investigation of the binding of 3-14C coumarin to rat serum proteins

Summary The binding of coumarin to serum proteins of the rat has been demonstrated. Of the total bound coumarin (37% of injected dose), 36% was bound to the slow and fast ₁ globulins, 11% to the post albumins, 10% to globulin and 9% to albumin.