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1.
J Anim Physiol Anim Nutr (Berl) ; 105(3): 462-469, 2021 May.
Artigo em Inglês | MEDLINE | ID: mdl-33469993

RESUMO

The aim of this study was to assess the effects of feeding immunized egg proteins (IEP) on the health and performance of newborn dairy calves. Sixty-four Holstein calves, both male and female, were divided over two treatments. Calves either received IEP or a placebo (PCB) in their colostrum and calf milk replacer (CMR) for the first 14 days of their life. Until day 49, CMR was offered at 15% of birth weight (BW), at 10% on days 49-57 and at 5% on days 57-63. In addition, calves received starter concentrate, chopped straw and water from 3 days old until 70 days old at the end of study. Individual CMR and concentrate intake were measured daily whilst BW was recorded weekly. Visual faecal scoring and health observations were conducted daily. Faecal samples were collected weekly up to 4 weeks and during the first 4 days of scouring to screen for presence of Cryptosporidium parvum, rotavirus, coronavirus, E. coli and Salmonella. Results indicated that feeding IEP increased BW (p < .05) at 42 and 56 days old, and BW also tended (p = .06) to be higher after weaning at 63-70 days old compared to the PCB group. When analysed using a repeated measures model, compared to feeding PCB, feeding IEP increased total concentrate consumption (p = .001) by 3.6kg/calf. Over the entire study, daily water intake was higher (p = .002) for the IEP group when compared with the PCB group. In the IEP group, 12 calves were scored as scouring whereas there were 14 calves in the PCB group. There were no significant differences between treatments in faecal pathogen load of neither healthy nor scouring calves. In conclusion, supplementing IEP during the first 14 days of calf life improved the performance of newborn calves. Further work is warranted to understand the mode of action of IEP in calves.


Assuntos
Doenças dos Bovinos/prevenção & controle , Diarreia/veterinária , Proteínas do Ovo/imunologia , Ração Animal , Animais , Animais Recém-Nascidos , Bovinos , Doenças dos Bovinos/epidemiologia , Doenças dos Bovinos/imunologia , Diarreia/epidemiologia , Diarreia/imunologia , Diarreia/prevenção & controle , Proteínas do Ovo/uso terapêutico , Fezes/química , Fezes/microbiologia , Fezes/parasitologia , Feminino , Incidência , Masculino , Aumento de Peso
2.
Anal Bioanal Chem ; 407(15): 4495-507, 2015 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-25912459

RESUMO

Growth-promoting agents are continually misused for increasing animal growth and fraudulent gain in the meat industry, yet detection rates from conventional targeted testing for drug residues do not reflect this. This is because testing currently relies on direct detection of drugs or related metabolites and administrators of such compounds can take adaptive measures to avoid detection through the use of endogenous or unknown drugs, and low dose or combined mixtures. New detection methods are needed which focus on the screening of biological responses of an animal to such growth-promoting agents as it has been demonstrated that genomic, proteomic and metabolomics profiles are altered by xenobiotic intake. Therefore, an untargeted proteomics approach using comparative two-dimensional gel electrophoresis (2DE) was carried out to identify putative proteins altered in plasma after treatment with oestradiol, dexamethasone or prednisolone. Twenty-four male cattle were randomly assigned to four groups (n = 6) for experimental treatment over 40 days, namely a control group of non-treated cattle, and three groups administered 17ß-oestradiol-3-benzoate (0.01 mg/kg, intramuscular), dexamethasone sodium phosphate (0.7 mg/day, per os) or prednisolone acetate (15 mg/day, per os), respectively. Plasma collected from each animal at day 25 post study initiation was subjected to proteomic analysis by 2DE for comparison of protein expression between treated and untreated animals. Analysis of acquired gel images revealed 22 plasma proteins which differed in expression by more than 50% (p < 0.05) in treated animals compared to untreated animals. Proteins of interest underwent identification by LC-MS/MS analysis and were found to have associated roles in transport, blood coagulation, immune response and metabolism pathways. In this way, seven proteins are highlighted as novel biomarker candidates including transthyretin which is shown to be significantly increased in all treatment groups compared to control animals and potentially may find use as global markers of suspect anabolic practice.


Assuntos
Biomarcadores/sangue , Proteínas Sanguíneas/análise , Bovinos/sangue , Proteômica/métodos , Detecção do Abuso de Substâncias/métodos , Espectrometria de Massas em Tandem/métodos , Anabolizantes/administração & dosagem , Animais , Biomarcadores/análise , Anticoncepcionais/administração & dosagem , Dexametasona/administração & dosagem , Dexametasona/análogos & derivados , Eletroforese em Gel Bidimensional/métodos , Estradiol/administração & dosagem , Estradiol/análogos & derivados , Glucocorticoides/administração & dosagem , Masculino , Prednisolona/administração & dosagem , Prednisolona/análogos & derivados
3.
Parasitol Res ; 111(4): 1707-13, 2012 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-22773043

RESUMO

In trematodes, there is a family of proteins which combine EF-hand-containing domains with dynein light chain (DLC)-like domains. A member of this family from the liver fluke, Fasciola hepatica-FhCaBP4-has been identified and characterised biochemically. FhCaBP4 has an N-terminal domain containing two imperfect EF-hand sequences and a C-terminal dynein light chain-like domain. Molecular modelling predicted that the two domains are joined by a flexible linker. Native gel electrophoresis demonstrated that FhCaBP4 binds to calcium, manganese, barium and strontium ions, but not to magnesium or zinc ions. The hydrophobic, fluorescent probe 8-anilinonaphthalene-1-sulphonate bound more tightly to FhCaBP4 in the presence of calcium ions. This suggests that the protein undergoes a conformational change on ion binding which increases the number of non-polar residues on the surface. FhCaBP4 was protected from limited proteolysis by the calmodulin antagonist W7, but not by trifluoperazine or praziquantel. Protein-protein cross-linking experiments showed that FhCaBP4 underwent calcium ion-dependent dimerisation. Since DLCs are commonly dimeric, it is likely that FhCaBP4 dimerises through this domain. The molecular model reveals that the calcium ion-binding site is located close to a key sequence in the DLC-like domain, suggesting a plausible mechanism for calcium-dependent dimerisation.


Assuntos
Motivos de Aminoácidos , Proteínas de Ligação ao Cálcio/genética , Fasciola hepatica/genética , Fasciola hepatica/metabolismo , Sequência de Aminoácidos , Animais , Dineínas/genética , Motivos EF Hand/genética , Metais/metabolismo , Modelos Moleculares , Dados de Sequência Molecular , Filogenia , Ligação Proteica , Conformação Proteica , Multimerização Proteica , Estrutura Terciária de Proteína , Análise de Sequência de DNA
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