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1.
Prev Med Rep ; 4: 242-7, 2016 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-27413689

RESUMO

We examined the feasibility and effectiveness of a cosmetic intervention program for frail older women. Thirty-nine older adults (83.0 ± 8.65 years) from two nursing homes in Tokyo were allocated to a cosmetic (intervention: n = 27) or a light-exercise (control: n = 12) group according to their nursing home residence. Both groups attended weekly classes over a 5-week period from May to June 2009. The program feasibility was examined using class participation, class attendance, and program adherence rates, while the effectiveness of the program was examined using the Geriatric Depression Scale (GDS) and participants' engagement in positive activities (i.e., engaging in social activities and going outside). The intervention group showed significantly higher rates on all feasibility measures than did the control group (class participation: 24.1% vs. 13.3%, class attendance: 75.5% vs. 32.6%, program adherence: 70.8% vs. 10.0%). Furthermore, the GDS scores decreased significantly in the intervention group, but not the control group. Although the change in GDS score was larger in the intervention group (- 1.30 ± 2.36) than in the control group (- 0.75 ± 3.53), the inter-group difference in this change was not significant. No significant differences were found between pre- and post-intervention positive activity rates in either group, or in the inter-group comparisons of changes in these rates. Overall, the cosmetic program was highly feasible and effective for improving the mental health of frail older women. However, further studies using longer intervention periods and larger samples would be needed to identify the program effectiveness.

2.
Orig Life Evol Biosph ; 41(5): 413-35, 2011 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-21562847

RESUMO

A good comprehension of the reactivity of peptides in aqueous solution is fundamental in prebiotic chemistry, namely for understanding their stability and behavior in primitive oceans. Relying on the stereoselectivity of the involved reactions, there is a huge interest in amino acid derivatives for explaining the spontaneous emergence of homochirality on primitive Earth. The corresponding kinetic and thermodynamic parameters are however still poorly known in the literature. We studied the reactivity of alanylalanine in acidic to neutral conditions as a model system. The hydrolysis into amino acids, the epimerization of the N-terminal residue, and the cyclization into diketopiperazine could be successfully identified and studied. This kinetic investigation highlighted interesting behaviors. Complex mechanisms were observed in very acidic conditions. The relative kinetic stability of the diastereoisomers of the dipeptide is highly dependent of the pH, with the possibility to dynamically destabilize the thermodynamically more stable diastereoisomers. The existence of the cyclization of dipeptides adds complexity to the system. On one hand it brings additional stereoselectivities; on the other hand fast racemization of heterochiral dipeptides is obtained.


Assuntos
Aminoácidos/química , Dipeptídeos/química , Água/química , Ciclização , Dicetopiperazinas/química , Planeta Terra , Concentração de Íons de Hidrogênio , Hidrólise , Cinética , Conformação Molecular , Soluções , Estereoisomerismo , Termodinâmica
3.
J Phys Chem B ; 115(14): 3959-63, 2011 Apr 14.
Artigo em Inglês | MEDLINE | ID: mdl-21417371

RESUMO

For the spontaneous generation of a Turing pattern, two intermediate species, an activator and an inhibitor, should be generated with the diffusion coefficient of the activator smaller than that of the inhibitor. The chlorite-iodide-malonic acid (CIMA) reaction that generates the activator, I(-), and inhibitor, ClO(2-), was performed in an open gel reactor. In order to lower the effective diffusivity of I(-), micelles of quaternary alkyl ammonium cationic amphiphiles and polymers having a quaternary alkyl ammonium cationic side chain were combined in the CIMA reaction system in an open gel reactor. A Turing pattern formation was observed with the addition of n-dodecyltrimethylammonium bromide. Employing the gel reactor prepared by the polymerization of a monomer having quaternary alkyl ammonium cationic side chains also leads to the generation of a Turing pattern. The micelles and polymers are believed to trap I(-) in their vicinity as a counterion to lower the effective diffusivity.

4.
Mar Biotechnol (NY) ; 10(4): 382-7, 2008.
Artigo em Inglês | MEDLINE | ID: mdl-18293038

RESUMO

Phospholipase A1 is a hydrolytic enzyme that catalyzes the removal of the acyl group from position 1 of glycerophospholipids to form 2-acyl lysophospholipids. Lysophospholipids are used in foods, cosmetics, and pharmaceuticals as surfactants. Novel forms of phospholipase A1 that function at low temperatures are desirable for use in lipophilic systems in food processing. However, there is currently little variety in the available sources of phospholipase A1. Given this situation, we screened the intestinal contents of marine animals for phospholipase A1-producing bacteria. Colonies that formed a halo on K28CP screening medium and that grew in K28 medium were cultured in liquid K28 medium, and the supernatant was retrieved for analysis. Phosphatidylcholine was added to the culture supernatant, and the product of the reaction was analyzed by using TLC. For culture supernatants that were able to generate lysophosphatidylcholine, synthetic phosphatidylcholines were added, and the site of the reaction was determined by analyzing the fatty acid compositions of the lysophosphatidylcholines generated by GLC. A bacterial isolate from a flatfish, which we named HFKI0020, was found to have phospholipase A1 activity at low temperatures. We determined that the isolate HFKI0020 is closely related to Pseudomonas by using 16S rDNA sequence analysis and by characterizing the isolate with respect to its physiologic and biochemical properties. From the intestinal contents of a marine fish, we successfully isolated a bacterium that secretes phospholipase A1 that is active at low temperatures.


Assuntos
Linguados/microbiologia , Fosfolipases A1/metabolismo , Pseudomonas/enzimologia , Pseudomonas/isolamento & purificação , Animais , Ácidos Graxos/química , Ácidos Graxos/metabolismo , Conteúdo Gastrointestinal/microbiologia , Biologia Marinha , Dados de Sequência Molecular , Filogenia , Pseudomonas/genética , Pseudomonas/crescimento & desenvolvimento , RNA Ribossômico 16S/genética , Temperatura
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