Gambling with Laws and Ethics in Cyberspace

The online world, referred to by some as cyberspace, offers a wide variety of activities: reading written content, interacting with others, engaging with multimedia and playing games of various kinds, and obtaining goods and services. However, many will ignore the written agreements and laws that govern these activities, and because of this, cyberspace can turn into a dangerous place. This chapter explores a small sample of legal and ethical issues that can arise in the interface between cyberspaces and real places for those not paying attention to such matters. The authors note how laws in the physical world remain applicable in the “virtual” world, requiring knowledge of jurisdiction, and discuss the potential for creating systems that protect the user from harm by embedding adherence to laws and providing support for ethics. The authors further explain how such embedding can work to address the complex legalities and potential need for intervention in addictive situations in online gambling

P1 variant antithrombins Glasgow (393 Arg to His) and Pescara (393 Arg to Pro) have increased heparin affinity and are resistant to catalytic cleavage by elastase Implications for the heparin activation mechanism

AbstractThe heparin affinity of normal and two P1 variants of antithrombin-III (AT) was studied by gradient elution with NaCl in Tris buffer on heparin-Sepharose. At pH 7.4 normal AT eluted art [Na+] 0.78 mol/l and the variants both showed increased affinity with AT Pescara eluting at [Na+] 0.86 mol/l and AT Glasgow at [Na+] 0.92 mol/l. We have earlier proposed a model for heparin activation in which the native state of AT maintains a salt bridge involving the P1 Arg-393 residue. Binding of heparin induces a higher heparin affinity conformation in which the salt bridge is disrupted to reveal the reactive centre for inhibition of thrombin. The Glasgow and Pescara variants, lacking a reactive centre P1 basic residue, would be unable to form this salt bridge, and we suggested that the high affinity conformation which they adopt as their native state would resemble the heparin induced conformation. To examine this model, we measured the heparin induced fluorescence of two P1 variants and tested the susceptibility of their reactive loops to catalytic cleavage. Both variants had fluorescence spectra indistinguishable from normal AT. In the absence of heparin, neither variant was more susceptible than normal to catalytic cleavage by human neutrophil elastase. These findings suggest that the conformation of these P1 variants is different to that of fully heparinized normal AT