When a visual field is presented for 40 or 80 msec and a subject is asked to judge the duration of the stimulus, judged duration is found to be less when the field is blank than when the field contains three letters, but is the same whether the three letters form a word or not. The perceived difference between "filled" and "blank" fields increases when the subject is required to memorize the presented letters. These data are consistent with a theory which assumes, inter alia, that a stimulus is analyzed by a visual information processor and a timer, that attention is shared between these processors, and that temporal judgments are based on the output of both processors.Most. if not all. theories about how temporal judgments are made contain the assumption that the perceived length of an interval depends on the "information" occurring during that interval. Because of this assumption. these theories depend on theories about how stimulus information is processed. stored. and retrieved within an organism. In the simplest case. where the stimulus consists. for example. of two lO-msec clicks separated by an interval. t , and the subject's task is to estimate t. the assumption has been made that the relevant stimulus information is the number of subjective pulses occurri ng during t ,

The cysteine proteinase superfamily is a source of natural structural variants of value in the investigation of mechanism. It has long been considered axiomatic that catalytic competence of these enzymes mirrors the generation of the ubiquitous catalytic site imidazolium-thiolate ion pair. We here report definitive evidence from kinetic studies supported by electrostatic potential calculations, however, that at least for some of these enzymes the ion pair state which provides the nucleophilic and acid-base chemistry is essentially fully developed at low pH where the enzymes are inactive. Catalytic competence requires an additional protonic dissociation with a common pKa value close to 4 possibly from the Glu50 cluster to control ion pair geometry. The pH dependence of the second-order rate constant (k) for the reactions of the catalytic site thiol groups with 4,4'-dipyrimidyl disulfide is shown to provide the pKa values for the formation and deprotonation of the (Cys)-S-/(His)-Im+H ion pair state. Analogous study of the reactions with 2,2'-dipyridyl disulfide reveals other kinetically influential ionizations, and all of these pKa values are compared with those observed in the pH dependence of kcat/Km for the catalyzed hydrolysis of N-acetylphenylalanylglycine 4-nitroanilide. The discrepancy between the pKa value for ion pair formation and the common pKa value close to 4 related to generation of catalytic activity is particularly marked for ficin (pKa 2.49 +/- 0.02) and caricain (pKa 2.88 +/- 0.02) but exists also for papain (pKa 3.32 +/- 0.01).