The active site and the phospholipid activation of rat liver lysosomal lipase are not stereospecific

The stereochemical specificity of lysosomal lipase of rat liver was investigated using enantiomeric triacylglycerol analogs, sn-1-alkyl-2,3-diacylglycerol and sn-3-alkyl-1,2-diacylglycerol as substrates. Lysosomal lipase utilized both substrates with equal rates. The dependence of the activity of lysosomal lipase on the stereoconfiguration of activating acidic phospholipid was also studied. Our results showed that both sn-3-phospholipids (diphosphatidylglycerol, phosphatidylserine) and sn-1-phospholipids (bis(monoacylglycero)phosphate (BMP) were efficient activators of this enzyme and thus the stereochemical configuration of the activating phospholipid is not important. Accordingly, the rat liver lysosomal lipase lacks stereospecificity with respect to both the triacylglycerol substrate and the acidic phospholipid activator.     

Family break-up in farmed silver foxes (Vulpes vulpes) housed in enlarged cage systems as families

We monitored the behaviour of farmed silver foxes housed in family units in enlarged cage systems from weaning until late October. Activity of family members, use of space available, and aggressive acts were recorded. Aggressiveness between family members increased from July until October, leading to a more scattered use of the available space. Furthermore, the mean activity level of family members increased, and the synchrony of activity decreased. We conclude that social tension in the fox families increased gradually during the autumn, leading to dispersion of the family members. Received in revised form: 22 October 2001 Electronic Publication