The responsibilities of the engaged bioethicist: Scholar,advocate, activist

The work of a bioethicist carries distinctive responsibilities. Alongside those of any worker, there are responsibilities associated with giving guidance to practitioners, policy makers and the public. In addition, bioethicists are professionally exposed to and required to identify situations of moral trouble, and as a result may find themselves choosing to work as advocates or activists, with responsibilities that are distinct from those generally acknowledged within academia. The requirement for bioethics to make normative judgements entails taking a stance, which means there cannot be a sharp line between ‘academic’ or ‘objective’ bioethics, and advocacy/activism, but a continuum of bioethicists’ engagement and an associated continuum of responsibilities.     

Location of the dihydroorotase domain within trifunctional hamster dihydroorotate synthetase

Mammalian dihydroorotase (DHOase, EC 3.5.2.3) is part of a trifunctional protein, dihydroorotate synthetase which catalyzes the first three reactions of de novo pyrimidine biosynthesis. We have subcloned a portion of the cDNA from the plasmid pCAD142 and obtained a nucleotide sequence which extends 2.1 kb in the 5' direction from the sequence encoding the aspartate transcarbamoylase (ATCase) domain at the 3'-end of the cDNA. The DHOase and ATCase domains have been purified from an elastase digest of the trifunctional protein and subjected to amino acid (aa) sequencing from their N termini. The sequence of the N-terminal 24 aa of the DHOase domain has been obtained and aligned with the cDNA sequence. The C-terminal residues of the DHOase domain have been identified as Leu followed by Val which, when taken with partial sequences of the CNBr fragments of this domain, defines the coding sequence of the active, globular DHOase domain released by proteolysis. Prediction of protein secondary structure from the deduced aa sequence showed that the DHOase domain (Mr 37,751) is separated from the C-terminal ATCase domain (Mr 34,323) by a bridging sequence (Mr 12,532) consisting of multiple beta-turns.