Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/0014-5793(82)80293-7 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Thermo-dependence of noxious mechanical heterotopic stimulation-dependent modulation of the spinal dorsal horn response to somatosensory stimulation.
J Integr Neurosci
December 2018
Centro de Biofísica y Neurociencias, CBN-UC, Facultad de Ciencias de la Salud, Universidad de Carabobo, Valencia, Venezuela.
Despite the frequent clinical hyper- or hypothermia cases, thermal-dependence of the endogenous pain modulation system at the spinal cord is not well understood. We evaluate spinal dorsal horn neuronal network responses during mechanical heterotopic noxious stimuli (HNS) at three different body temperatures (34; 37 or 40°C) by measuring lumbar cord dorsum potentials activated by electrical stimulation of the ipsilateral sural nerve in adult thiopental anesthetized rats. A noxious clamp was applied randomly to the tail, right hindpaw, right forepaw, muzzle and left forepaw.
View Article and Find Full Text PDFThe cold-adapted γ-glutamyl-cysteine ligase from the psychrophile Pseudoalteromonas haloplanktis.
Biochimie
September 2014
Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli Federico II, Via S. Pansini 5, 80131 Napoli, Italy. Electronic address:
A recombinant γ-glutamyl-cysteine ligase from the psychrophile Pseudoalteromonas haloplanktis (rPhGshA II) was produced and characterised. This enzyme catalyses the first step of glutathione biosynthesis by forming γ-glutamyl-cysteine from glutamate and cysteine in an ATP-dependent reaction. The other ATP-dependent enzyme, glutathione synthetase (rPhGshB), involved in the second step of the biosynthesis, was already characterised.
View Article and Find Full Text PDFCatalase is well known to eliminate H2O2 in cells and reduces the toxicity of peroxide compounds. A catalase gene HpCat1 of methylotrophic yeast Hansenula polymorpha without the part coding the native signal peptide was cloned into expression vector pYM3165 and then integrated into genome of Pichia pastoris GS115 by electroporation. The result of the enzyme activity assay and SDS-PAGE demonstrated that the recombinant protein (HpCAT1) of H.
View Article and Find Full Text PDFTemperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases.
Biochimie
September 2012
Laboratory of Biochemistry, Center for Protein Engineering, University of Liège, B-4000 Liège-Sart Tilman, Belgium.
The functional and structural adaptations to temperature have been addressed in homologous chloride-dependent α-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete. This series covers nearly all temperatures encountered by living organisms. We report a striking continuum in the functional properties of these enzymes coupled to their structural stability and related to the thermal regime of the source organism.
View Article and Find Full Text PDFExpression, characterization and 2,4,6-trichlorophenol degradation of laccase from Monilinia fructigena.
Mol Biol Rep
April 2012
College of Horticulture, Nanjing Agricultural University, Nanjing, 210095, China.
A novel laccase gene from Monilinia fructigena was synthesized chemically according to the yeast bias codon and integrated into the genome of Pichia pastoris GS115 by electroporation. The expressed enzyme was recovered from the culture supernatant and purified. The result of enzyme activity assay and SDS-PAGE demonstrated that the recombinant laccase was induced and extracellularly expressed in P.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!