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1.
J Dairy Res ; 82(3): 272-8, 2015 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-25876988

RESUMEN

An experiment was conducted during 6 weeks to evaluate effects of a reduced dietary level of protein-rich concentrates in a moderate dairy production system on cows' performance, protein efficiency and milk quality including fatty acid profiles. Twenty-three lactating cows (Swiss Fleckvieh) were assigned either to a group receiving on average 2.4 kg/d individually fed concentrates (Prot+, n = 12) or to a group receiving no individually fed concentrates (Prot-, n = 11). All cows had ad-libitum access to a total mixed ration (TMR) mainly based on grass and maize silage, hay and little potatoes and soybean cake. In weeks 4-6 of the experiment, part of the hay was excluded from the TMR, and fed separately in the morning. Individual feed intake and milk yield were recorded during weeks 3 and 6 of the experiment; at the same time feed, faeces and milk samples were collected twice per week for analyses. Data were processed in linear mixed models. Omission of individual concentrates in Prot- was fully compensated by higher roughage intake in terms of dry matter. Crude protein (CP) and net energy intake was almost maintained. Despite a lower apparent CP digestibility in Prot-, the ratio of milk protein to ingested CP was the same in both groups, indicating a higher ruminal utilisation of degraded CP in Prot-. This corresponded with lower milk urea concentrations in Prot-. Milk quality was affected in terms of lower concentrations of linoleic and conjugated linoleic acid in milk fat of Prot-. Concentrations of odd- and branched-chain fatty acids in milk were increased in Prot-. Sequential offer of hay and TMR did not lead to considerable effects in intake, efficiency and milk quality. In conclusion, the results indicate that the efficiency of feed protein utilisation for milk protein is not impaired if concentrates are reduced in a moderate- to low-input dairy production system.


Asunto(s)
Bovinos , Dieta/veterinaria , Fibras de la Dieta/administración & dosificación , Proteínas en la Dieta/administración & dosificación , Proteínas de la Leche/análisis , Leche/química , Alimentación Animal , Fenómenos Fisiológicos Nutricionales de los Animales , Animales , Industria Lechera , Proteínas en la Dieta/metabolismo , Digestión , Ácidos Grasos/análisis , Femenino , Lactancia , Ácido Linoleico/análisis , Ácidos Linoleicos Conjugados/análisis , Agricultura Orgánica , Suiza , Urea/análisis
2.
Sci Rep ; 4: 5380, 2014 Jun 20.
Artículo en Inglés | MEDLINE | ID: mdl-24946853

RESUMEN

The interface structure of graphene with thermally evaporated metal oxide layers, in particular molybdenum trioxide (MoO3), is studied combining photoemission spectroscopy, sheet resistance measurements and organic light emitting diode (OLED) characterization. Thin (<5 nm) MoO3 layers give rise to an 1.9 eV large interface dipole and a downwards bending of the MoO3 conduction band towards the Fermi level of graphene, leading to a near ideal alignment of the transport levels. The surface charge transfer manifests itself also as strong and stable p-type doping of the graphene layers, with the Fermi level downshifted by 0.25 eV and sheet resistance values consistently below 50 Ω/sq for few-layer graphene films. The combination of stable doping and highly efficient charge extraction/injection allows the demonstration of simplified graphene-based OLED device stacks with efficiencies exceeding those of standard ITO reference devices.

3.
Drug Metab Dispos ; 40(5): 1041-50, 2012 May.
Artículo en Inglés | MEDLINE | ID: mdl-22344701

RESUMEN

Panobinostat (LBH589) is a novel pan-deacetylase inhibitor that is currently being evaluated in phase III clinical trials for treatment of Hodgkin's lymphoma and multiple myeloma. Under catalysis of recombinant human CYP3A4 and CYP2D6 coexpressed with human cytochrome P450 reductase in Escherichia coli JM109, five metabolites of panobinostat were produced via whole-cell biotransformation. The structures of the metabolites were elucidated with the spectroscopic methods mass spectrometry (MS) and NMR and revealed an oxidative cyclization of the ethyl-amino group to the methylindole moiety. The MS(2) spectrum of the cyclized metabolite showed a base peak, where the closed ring is reopened and that, taken as sole base for structure proposals, would have lead to wrong conclusions. The metabolites were substantially less potent deacetylase inhibitors than the parent compound.


Asunto(s)
Antineoplásicos , Citocromo P-450 CYP2D6/metabolismo , Citocromo P-450 CYP3A/metabolismo , Inhibidores de Histona Desacetilasas , Ácidos Hidroxámicos , Antineoplásicos/química , Antineoplásicos/metabolismo , Antineoplásicos/farmacología , Biocatálisis , Biotransformación , Cromatografía Líquida de Alta Presión , Ciclización , Citocromo P-450 CYP2D6/genética , Citocromo P-450 CYP3A/genética , Escherichia coli/genética , Inhibidores de Histona Desacetilasas/química , Inhibidores de Histona Desacetilasas/metabolismo , Inhibidores de Histona Desacetilasas/farmacología , Humanos , Ácidos Hidroxámicos/química , Ácidos Hidroxámicos/metabolismo , Ácidos Hidroxámicos/farmacología , Indoles , Conformación Molecular , Panobinostat , Espectrometría de Masas en Tándem
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