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1.
J Aging Soc Policy ; 24(1): 62-76, 2012.
Article in English | MEDLINE | ID: mdl-22239282

ABSTRACT

If job training has positive impacts on worker satisfaction, then job training can have desirable consequences for an organization that result both directly through its effects on productivity and indirectly through its effects on job satisfaction. Furthermore, the aging of the workforce implies that older workers will become increasingly important to firms and to the economy. This study, therefore, seeks to examine the relationship between job training and job satisfaction, focusing in particular on U.S. workers born in 1964 or earlier. The results of ordered logit regression analysis indicate that availability and quality of training received directly affect job satisfaction.


Subject(s)
Aging , Inservice Training/statistics & numerical data , Job Satisfaction , Personnel Management , Adult , Aged , Female , Humans , Male , Middle Aged , Retirement , Time Factors
2.
J Aging Soc Policy ; 21(1): 17-30, 2009.
Article in English | MEDLINE | ID: mdl-19197606

ABSTRACT

International comparisons of the economic impact of population aging across nations can give valuable insights regarding which policies are most effective in addressing aging-related economic issues. Traditional old-age dependency ratios, by not accounting for differences in labor force participation rates, can be misleading. A new measure, the difference between an age group's share of total employment and its share of the total adult population, is developed and shown to be empirically sensitive to different policy actions. The analysis is built upon readily available and comparable International Labour Organization age-group data on population and labor force participation rates.


Subject(s)
Aging , Cross-Cultural Comparison , Economics/statistics & numerical data , Employment/statistics & numerical data , Population Dynamics , Aged , Demography , Economics/trends , Humans
3.
Theor Appl Genet ; 111(1): 44-9, 2005 Jun.
Article in English | MEDLINE | ID: mdl-15883792

ABSTRACT

The production of resistant soybean [Glycine max (L.) Merr.] cultivars is the most effective means for controlling losses from soybean cyst nematode (SCN) (Heterodera glycines Ichinohe). The major resistance gene in most SCN resistance sources is rhg1, which has been mapped as a quantitative trait locus onto linkage group G. Our objective was to determine whether the SCN resistance sources PI 437654 and PI 88788 have different functional alleles at rhg1 based on resistance phenotypes. Populations segregating for resistance alleles at rhg1 from both PI 88788 and PI 437654 and at Rhg4, a second SCN resistance gene from PI 437654, were developed. These populations were screened for resistance to the H. glycines inbred isolates PA3 (HG type 7) and TN14 (HG type 1.2.5.7) in the greenhouse and evaluated with molecular markers linked to both rhg1 and Rhg4. Each isolate test was repeated, and the evaluations were done on a single-plant and a line-mean basis in Test 1, and solely on a single-plant basis in Test 2. Across two tests with the TN14 isolate, plants with the PI 437654 allele for a marker linked to rhg1 had significantly (P<0.0001) less SCN reproduction than plants carrying the PI 88788 allele. A marker linked to Rhg4, however, was not significantly associated with resistance to TN14. Across two tests with the PA3 isolate, alleles of rhg1 from both sources gave a resistant reaction, although plants homozygous for the PI 88788 allele had significantly (P<0.05) greater resistance than plants with the PI 437654 allele. The marker allele from PI 437654 linked to Rhg4 was significantly (P<0.0005) associated with greater resistance than the PI 88788 allele in both PA3 tests, and resistance was dominant. There was a significant interaction between alleles at rhg1 and Rhg4 in both PA3 tests. These results suggest that PI 437654 and PI 88788 each have a different functional SCN resistance allele at or close to rhg1. These allelic differences have implications that breeders should consider before incorporation into cultivars.


Subject(s)
Alleles , Genes, Plant/genetics , Glycine max/genetics , Immunity, Innate/genetics , Plant Diseases/parasitology , Tylenchoidea , Analysis of Variance , Animals , Genetic Markers/genetics , Plant Diseases/genetics , Reproduction/genetics , Reproduction/physiology , Glycine max/physiology
4.
Appl Environ Microbiol ; 69(10): 6272-9, 2003 Oct.
Article in English | MEDLINE | ID: mdl-14532091

ABSTRACT

The introduction of acellular pertussis vaccines has greatly enhanced the safety profile of vaccines to prevent whooping cough. Pertussis toxin (Ptx) is one component produced by Bordetella pertussis that is contained in all of these vaccines, either in combination with other known pertussis virulence factors or as the sole pertussis component, combined with tetanus and diphtheria toxoids. A hydrogen peroxide toxoid of Ptx has been shown to be efficacious in preventing pertussis infections in a mass vaccination trial and is presently licensed in the United States and Europe (B. Trollfors, J. Taranger, T. Lagergard, L. Lind, V. Sundh, G. Zackrisson, C. U. Lowe, W. Blackwelder, and J. B. Robbins, N. Engl. J. Med. 333:1045-1050, 1995). The industrial production of Ptx can be performed through the cultivation of B. pertussis in well-defined growth media, in which the components can be well characterized and their origins can be documented. Once the bacteria are removed from the culture, Ptx can be isolated from the supernatant and purified by using the technique described by Sekura et al. (R. D. Sekura, F. Fish, C. R. Manclark, B. Meade, and Y. L. Zhang, J. Biol. Chem. 258:14647-14651, 1983). The only drawback of this procedure, which combines two affinity chromatography steps, one with Blue Sepharose and a second with matrix-bound bovine fetuin (BF), is the source and purity of the BF. Concern about vaccine preparations that may possibly risk contamination by material associated with bovine spongioform encephalopathy has continued to increase. We thus sought a replacement for the BF affinity chromatography and, more specifically, for the glycosidic moiety on BF. We describe here the identification of a seven-amino-acid peptide that mimics the glycosidic moiety on BF to which Ptx binds. Furthermore, we have constructed an affinity column containing this peptide that can be used to replace BF in Ptx purification. Finally, we used the X-ray crystallographic structure of Ptx bound to the oligosaccharide moiety of BF as a scaffold and replaced the oligosaccharide with the peptide.


Subject(s)
Molecular Mimicry , Peptides/chemistry , Pertussis Toxin/chemistry , Pertussis Toxin/isolation & purification , alpha-Fetoproteins/chemistry , Amino Acid Sequence , Animals , Antibodies, Bacterial/immunology , Binding Sites , Bordetella pertussis/immunology , Bordetella pertussis/metabolism , CHO Cells , Cattle , Chromatography, Affinity/methods , Cricetinae , Crystallography, X-Ray , Humans , Models, Molecular , Molecular Sequence Data , Peptide Library , Peptides/chemical synthesis , Peptides/immunology , Peptides/metabolism , Pertussis Toxin/immunology , Pertussis Vaccine/administration & dosage , Pertussis Vaccine/immunology , Whooping Cough/prevention & control
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