Darwinian functions and Freudian motivations

Badcock, and Nesse and Lloyd, have argued that there are important points of agreement between Freud's theory of the mind and a theory of mind suggested by adaptive reasoning. Buller, on the other hand, draws attention to the need to avoid confusing an adaptive rationale with an unconscious motivation. The present paper attempts to indicate what role adaptive reasoning might have to play in justifying psychoanalytic claims. First, it is argued that psychoanalytic claims cannot be justified by the clinical experience of psychoanalysts alone. It is urged that, to avoid interpretative proliferation, it is necessary to base interpretation on some theory which is external to psychoanalysis. Next, Buller's reservations about using adaptive reasoning to justify claims about a personal unconscious, are summarized. Then an argument for the existence of a personal unconscious, is offered, based on experimental evidence from Gur and Sackeim. Then it is argued that adaptive reasoning, though it cannot itself provide evidence for the existence of any psychological mechanism, can valuably guide the search for such evidence. It is argued that such an approach has borne fruit, both in biology generally and specifically in psychology. Finally, it is argued that psychoanalysis is important enough to justify such a research project.     

A novel human phosphotransferase highly specific for adenosine.

A novel nucleoside phosphotransferase, referred to as adenosine phosphotransferase (Ado Ptase), was partially purified 1230-fold from human placenta. This enzyme differed from other known nucleoside phosphotransferases in its substrate specificity. Using AMP as the phosphate donor, it readily phosphorylated Ado. Changes in the sugar moiety were tolerated. dAdo and ddAdo were phosphate acceptors and dAMP was a donor. No other nucleotide or nucleoside common in nature displayed appreciable activity as donor or acceptor substrate, respectively. In the absence of nucleoside, the enzyme catalyzed the hydrolysis of AMP, typical of other nucleoside phosphotransferases. However, in the presence of Ado, little, if any, hydrolysis occurred. Ado Ptase had an absolute requirement for a metal cation, with Mg2+ and, to a lesser extent, Mn2+ fulfilling this requisite. The apparent Km for Ado was 0.2 mM. However, the donor AMP displayed cooperativity in both transfer and hydrolytic reactions. This cooperativity was eliminated by nucleotides, 2,3-diphosphoglycerate, and inorganic phosphate. ADP and 2,3-diphosphoglycerate were especially potent. In the presence of these effectors, the apparent Km for AMP was 3.0 mM in the transfer reaction and 4.0 mM in the hydrolytic reaction. Kinetic data suggest that there are two nucleotide binding sites on Ado Ptase, one for the donor, the other for an effector. AMP appeared to bind to both sites. Although this novel enzyme might play a role in the anabolism of nucleoside analogues, the normal physiological role of this nucleoside phosphotransferase is not understood.