0000000000262898

AUTHOR

Bruna Pleše

showing 2 related works from this author

ATP distribution and localization of mitochondria in Suberites domuncula (Olivi 1792) tissue

2011

SUMMARY The metabolic energy state of sponge tissue in vivo is largely unknown. Quantitative bioluminescence-based imaging was used to analyze the ATP distribution of Suberites domuncula (Olivi 1792) tissue, in relation to differences between the cortex and the medulla. This method provides a quantitative picture of the ATP distribution closely reflecting the in vivo situation. The obtained data suggest that the highest ATP content occurs around channels in the sponge medulla. HPLC reverse-phase C-18, used for measurement of ATP content, established a value of 1.62 μmol ATP g–1 dry mass in sponge medulla, as opposed to 0.04 μmol ATP g–1 dry mass in the cortex, thus indicating a specific and…

PhysiologyProtein subunitIn situ hybridizationAquatic ScienceBiologyMitochondrionAdenosine TriphosphateImage Processing Computer-AssistedAnimalsMolecular BiologyChromatography High Pressure LiquidIn Situ HybridizationEcology Evolution Behavior and SystematicsMedullaArginine KinaseArginine kinaseATP distribution; mitochondria; imaging bioluminescence; HPLC; Porifera; Suberites domunculabiology.organism_classificationImmunohistochemistryMitochondriaSuberites domunculaSpongeBiochemistryOrgan SpecificityInsect Sciencebiology.proteinAnimal Science and ZoologyMitochondrion localizationEnergy MetabolismSuberitesJournal of Experimental Biology
researchProduct

Strombine dehydrogenase in the demosponge Suberites domuncula: Characterization and kinetic properties of the enzyme crucial for anaerobic metabolism

2008

Previously, the cDNA and the respective gene for a presumed tauropine dehydrogenase (TaDH) from Suberites domuncula (GenBank accession nos. AM712888, AM712889) had been annotated. The conclusion that the sequences encode a TaDH had been inferred from the 68% identity with the TaDH protein from the marine demosponge Halichondria japonica. However, subsequent enzymatic assays shown here indicate that the presumed S. domuncula opine dehydrogenase is in fact a strombine dehydrogenase (StDH). The enzyme StDH is highly specific for glycine and is inhibited by an excess of the substrate pyruvate. Besides kinetic data, we report in this study also on the predicted tertiary and quaternary structure …

Models MolecularPhysiologyGlycineDehydrogenaseBiochemistrySubstrate SpecificityComplementary DNAPyruvic AcidAnimalsAnaerobiosisProtein Structure QuaternaryMolecular Biologychemistry.chemical_classificationOxidoreductases Acting on CH-NH Group DonorsStrombine dehydrogenasebiologyTauropine dehydrogenaseAnaerobic metabolism; Demospongiae; Opine dehydrogenase; Strombine dehydrogenase; Suberites domunculabiology.organism_classificationProtein Structure TertiarySuberites domunculaKineticsEnzymechemistryBiochemistryGlycineFemaleProtein quaternary structureProtein MultimerizationSuberites
researchProduct