Declines in divergent thinking with age: Cross-sectional, longitudinal, and cross-sequential analyses.

Six measures of divergent thinking were administered to 825 men ranging in age from 17 to 101 over the period from 1959 to 1972; repeat administrations were given to a subset of 278 men after a 6-year interval. Cross-sectional analyses showed curvilinear trends, with an increase in scores for men under 40 and a decline thereafter. Repeated measures analyses on subjects initially aged 33 to 74 generally replicated this finding, whereas cross-sequential analyses suggested a decline for all cohorts tested at a later time. Additional analyses suggested that not all of the decline could be attributed to reduced speed of response production. These longitudinal findings confirm earlier cross-sectional reports of decline in divergent thinking abilities with age. (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Contingent suppression of tolerance to the "anorexigenic" effect of haloperidol.

Whether tolerance develops to the "anorexia" induced by haloperidol (HAL) was determined. Rats were given HAL (2.5 or 5 mg/kg) either before or after access to milk for 53 days. Controls were given injections of saline. On Day 54, when all groups received pretest injections of the drug, only rats previously given posttest injections of HAL were tolerant. The absence of tolerance in rats previously given pretest injections suggests that tolerance is suppressed when rats are given access to food in the drugged state. It is concluded that tolerance develops to HAL as a result of pharmacological exposure but is suppressed by the "anhedonic" effect of the drug. The relevance of these findings to the role of reinforcement in behavioral tolerance is briefly discussed. (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Kinetics of phenol oxidation in a trickle bed reactor over active carbon catalyst

The wet air oxidation of phenol over a commercial active carbon catalyst was studied in a trickle bed reactor (TBR) in the temperature and oxygen partial pressure ranges of 120–160 °C and 0.1–0.2 MPa, respectively. The performance of the active carbon was compared in terms of phenol and COD destruction. The weight change of active carbon due to reaction was also measured. Finally, oxic phenol adsorption isotherms were assessed in batch conditions at 25, 125 and 160 °C. In order to use the conversion data obtained from the TBR for a kinetic study, special care was taken to check the kinetic control in the TBR experiments. Several kinetic models including power law or Langmuir–Hinshelwood expressions were considered to describe the catalytic oxidation of phenol over active carbon. The simple power law model with first order dependence on both phenol and oxygen concentration predicted satisfactorily the experimental data not only over the entire range of operating conditions studied, but also outside its validity range. Copyright © 2005 Society of Chemical Industry     

Surface Morphology of Heat-Treated Ceramic Thin Films

The morphology of surfaces of several ceramic materials has been examined using transmission electron microscopy. The approach used was to prepare a sample for examination in the microscope, carefully clean it, and then heat-treat it. In the case of the oxides studied (alumina and spinel) the samples were heated in air; the non-oxides (α-SiC and β -SiC) were annealed under vacuum. The morphology in all but one case was such that the surface faceted parallel to the nearest low-index plane to give well-defined terraces; these were separated by ledges which also tended to facet parallel to the traces of low-index planes. The exception was the {1100} alumina surface, which appears to be unstable in air at temperatures close to 1400°C. A computer program using a multislice approach was used to estimate the height of the steps on the (0001) surface; the step heights appear to be multiples of the c lattice parameter. A reconstruction of this surface as a result of this heat treatment is also proposed.     

6-Phospho-{beta}-galactosidases of Gram-positive and 6-phospho-{beta}-glucosidase B of Gram-negative bacteria: comparison of structure and function by kinetic and immunological methods and mutagenesis of the lacG gene of staphylococcus aureus

The 6-phospho-ß-galactosidase of Staphylococcus aureus,Lactococcus lactis and Lactobacillus casei and 6-phospho-ßglucosidaseB of Escherichia coli build a subfamily inside a greater enzymefamily, named the glycosal hydrolase family 1, which, hi addition,contains nine ß-glycosidases of different origins.Kinetic and immunological evidence is provided in this reportwhich strengthens the relationship of the four 6-phospho-ß-glycosidases.It is shown that the 6-phospho-ß-galactosidases and6-phospho-ß-glucosidase B are able to split aromaticß-galactoside phosphates and ß-glucosidephosphates. The turnover numbers of hydrolysis of substrateswith different epimerization at C-4 of the glycon vary up to15-fold only. Two polydonal antisera, one derived against thenative 6-phospho-ß-galactosidase from S.aureus andthe other derived against the 6-phospho-ß-glucosidaseB, cross-reacted with both enzymes. Peptides of the proteinswere separated by reverse phase HPLC. The cross-reacting peptideswere sequenced and shown to be localized at almost the sameposition in the aligned primary structures of both enzymes.An insertion of nine amino adds near these antigenic domainsis unique for the 6-phospho-ß-glycosidases and missingwithin the sequences of the ß-glycoside-specific membersof the family. The lacG gene of a 6-phospho-ß-galactosidasenegative S.aureus mutant was doned into E.coli and sequenced.In the totally inactive mutant protein only the glycine at position332 was changed to an arginine. This amino acid is part of thesequence insertion near the antigenic domain reacting with bothantisera. These data support the assumption that the regionis of great importance for the function of the enzymes and thatit is possible it determines the specificity of the phosphorylatedform of the substrates. In addition, the 6-phospho-ß-galactosidaseof S.aureus was modified by sitedirected mutagenesis of thecorresponding lacG gene hi order to replace residues Glul60and Glu375, which were suspected of being involved hi the generalacid catalysis of substrate hydrolysis, with glutamine residues.The mutant protein 160EQ retained some catalytic activity whilethe protein 375EQ was totally inactive. Glu375 is the activesite nudeophile of the 6-phospho-ß-galactosidase ofS.aureus. It is located in the sequence motif ENG where Glu358was identified as the catalytkally active nudeophile hi theß-glucosidase of Agrobacterium.