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1.
J Dairy Sci ; 100(11): 9392-9401, 2017 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-28918156

RESUMO

Heat treatment of colostrum is performed on modern dairy farms to reduce pathogenic contamination before hand-feeding the colostrum to newborn calves; however, limited data are available concerning effects of heat treatment on biologically active proteins in colostrum. The objective of this exploratory study was to investigate effects of heat treatment and length of heat treatment on colostrum protein profile. Colostrum samples were collected from Holstein cows within 12 h after parturition and assigned to the following groups: heat treatment at 60°C for 0 (untreated control), 30, 60, or 90 min. Samples were fractionated using acid precipitation, followed by ultracentrifugation and ProteoMiner (Bio-Rad Laboratories, Hercules, CA) treatment, and tandem-mass tagging was used to comparatively assess the low abundance protein profile. A total of 162 proteins were identified with more than 2 peptides in the low abundance protein enriched fraction. Of these, 62 differed in abundance by more than 2-fold in heat-treated samples compared with the unheated control. The majority of proteins affected by heat treatment were involved in immunity, enzyme function, and transport-related processes; affected proteins included lactadherin, chitinase-3-like protein 1, and complement component C9. These results provide a foundation for further research to determine optimum heat treatment practices to ensure newborn calves are fed colostrum-containing proteins with the highest nutritional and biological value.


Assuntos
Bovinos/fisiologia , Colostro/química , Temperatura Alta , Proteoma , Animais , Feminino , Imunoglobulina G , Gravidez
2.
Neuroscience ; 242: 78-84, 2013 Jul 09.
Artigo em Inglês | MEDLINE | ID: mdl-23558090

RESUMO

Relay cells of dorsal lateral geniculate nucleus (LGN) receive a Class 1 glutamatergic input from the retina and a Class 2 input from cortical layer 6. Among the properties of Class 2 synapses is the ability to activate metabotropic glutamate receptors (mGluRs), and mGluR activation is known to affect thalamocortical transmission via regulating retinogeniculate and thalamocortical synapses. Using brain slices, we studied the effects of Group I (dihydroxyphenylglycine) and Group II ((2S,2'R,3'R)-2-(2',3'-dicarboxycyclopropyl)glycine) mGluR agonists on retinogeniculate synapses. We showed that both agonists inhibit retinogeniculate excitatory postsynaptic currents (EPSCs) through presynaptic mechanisms, and their effects are additive and independent. We also found high-frequency stimulation of the layer 6 corticothalamic input produced a similar suppression of retinogeniculate EPSCs, suggesting layer 6 projection to LGN as a plausible source of activating these presynaptic mGluRs.


Assuntos
Corpos Geniculados/fisiologia , Inibição Neural/fisiologia , Receptores de Glutamato Metabotrópico/fisiologia , Retina/fisiologia , Transmissão Sináptica/fisiologia , Animais , Córtex Cerebral/fisiologia , Ciclopropanos/farmacologia , Agonistas de Aminoácidos Excitatórios/farmacologia , Potenciais Pós-Sinápticos Excitadores/efeitos dos fármacos , Potenciais Pós-Sinápticos Excitadores/fisiologia , Corpos Geniculados/efeitos dos fármacos , Glicina/análogos & derivados , Glicina/farmacologia , Camundongos , Vias Neurais/efeitos dos fármacos , Vias Neurais/fisiologia , Estimulação Luminosa , Receptores de Glutamato Metabotrópico/agonistas , Resorcinóis/farmacologia , Retina/efeitos dos fármacos , Transmissão Sináptica/efeitos dos fármacos , Tálamo/fisiologia , Vias Visuais/fisiologia
3.
Int J Biochem Cell Biol ; 34(6): 625-31, 2002 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-11943593

RESUMO

A single-chained protein designated solenin was isolated from Solenognathus hardwickii, a fish used as traditional Chinese medicinal material. Solenin was capable of inhibiting translation in a cell-free rabbit reticulocyte lysate system with an IC(50) of 2 microM and expressing a ribonuclease activity of 0.8U/mg toward yeast transfer RNA, but it lacked N-glycosidase activity characteristic of ribosome inactivating proteins Solenin exhibited a molecular weight of 18kDa and possessed an N-terminal sequence AHDAEVNEVKAQVAA. The protein was adsorbed on three types of chromatographic media: Affi-gel blue gel, CM-Sepharose and Mono S. It was devoid of antifungal and lectin activities.


Assuntos
Biossíntese de Proteínas/efeitos dos fármacos , Sequência de Aminoácidos , Animais , Sistema Livre de Células , Cromatografia de Afinidade , Cromatografia por Troca Iônica , Relação Dose-Resposta a Droga , Eletroforese em Gel de Poliacrilamida , Proteínas de Peixes , Peixes , Medicina Tradicional Chinesa , Dados de Sequência Molecular , Peso Molecular , Proteínas , Coelhos , Reticulócitos/metabolismo , Ribonucleases/metabolismo , Homologia de Sequência de Aminoácidos
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