123 research outputs found

    Revisiting tectonic corrections applied to Pleistocene sea-level highstands

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    Tectonic displacement contaminates estimates of peak eustatic sea level (and, equivalently, minimum continental ice volumes) determined from the elevation of Quaternary interglacial highstand markers. For sites at which a stratigraphic or geomorphic marker of peak Marine Isotope Stage (MIS) 5e sea level exists, the standard approach for estimating local tectonic uplift (or subsidence) rates takes the difference between the elevation of the local highstand marker and a reference MIS 5e eustatic value, commonly chosen as +6 m, and divides by the age of the marker. The resulting rate is then applied to correct the elevation of all other local observed sea-level markers for tectonic displacement, including peak highstands of different ages (e.g., MIS 5a, MIS 5c and MIS 11), under the assumption that the tectonic rate remained constant over those periods. This approach introduces two potentially significant errors. First, the peak eustatic value adopted for MIS 5e in most previous studies (i.e., +6 m) is likely incorrect. Second, local peak sea level during MIS 5e is characterized by significant departures from eustasy due to glacial isostatic adjustment in response to both successive glacial–interglacial cycles and excess polar ice-sheet melt relative to present day values. We use numerical models of glacial isostatic adjustment that incorporate both of these effects to quantify the plausible range of the combined error and show that, even at sites far from melting ice sheets, local peak sea level during MIS 5e may depart from eustasy by 2–4 m, or more. We also demonstrate that the associated error in the estimated tectonic rates can significantly alter previous estimates of peak eustatic sea level during Quaternary highstands, notably those associated with earlier interglacials (e.g., MIS 11)

    Biochemical Characterization of a Filtered Synaptoneurosome Preparation from Guinea Pig Cerebral Cortex: Cyclic Adenosine 3’:5’-Monophosphate-generating Systems, Receptors, and Enzymes

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    A particulate preparation was obtained by low speed centrifugation of guinea pig cerebral cortical homogenates prepared with a Krebs-Henseleit buffer. Light microscopic examination, using a reflected light differential interference contrast system, reveals the presence of intact neurons, axonal fragments, glial cells, and erythrocytes along with an abundance of small spherical entities (diameter about 1.1 μm) and snowman-shaped entities (diameter of larger sphere about 1.1 μm, diameter of attached smaller sphere about 0.6 μm). Many unattached smaller spherical entities are also present (diameter about 0.6 μm). Pressure filtration through 5 or l0-μm Millipore filters, followed by low speed centrifugation and resuspension, removes most of the larger entities to afford a suspension composed mainly of the small spherical and snowman-shaped entities. Electron microscopic examination reveals the presence of many synaptosomes with attached resealed postsynaptic entities. It is proposed that these correspond to the snowman-shaped entities to be termed synaptoneurosomes. Accumulations of cyclic AMP elicited by 2-chloroadenosine and histamine, and by combinations of 2-chloroadenosine, histamine, norepinephrine, and forskolin, are lower in filtered than in unfiltered preparations, whereas accumulations elicited by forskolin are unchanged. Levels of adenylate cyclase are reduced by filtration, whereas levels of phosphodiesterase are unchanged. Filtration reduces levels of markers for whole cells and endothelial cells, whereas neuronal markers such as acetylcholinesterase activity and norepinephrine uptake are increased. Levels of S-100 protein, a marker for glial cells, are not significantly decreased. There is no apparent change in the density of many receptors or ion channels. Levels of A1-adenosine and H1-histamine receptors are increased, whereas levels of so-called peripheral benzodiazepine-binding sites are decreased

    Geobiology of a lower Cambrian carbonate platform, Pedroche Formation, Ossa Morena Zone, Spain

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    The Cambrian Pedroche Formation comprises a mixed siliciclastic-carbonate succession recording subtidal deposition on a marine platform. Carbonate carbon isotope chemostratigraphy confirms previous biostratigraphic assignment of the Pedroche Formation to the Atdabanian regional stage of Siberia, correlative to Cambrian Series 2. At the outcrop scale, thrombolitic facies comprise ~. 60% of carbonate-normalized stratigraphy and coated-grains another ~. 10%. Petrographic point counts reveal that skeletons contribute at most 20% to thrombolitic inter-reef and reef-flank lithologies; on average, archaeocyath clasts make up 68% of skeletal materials. In contrast, petrographic point counts show that skeletons comprise a negligible volume of biohermal and biostromal thrombolite, associated nodular carbonate facies, and ooid, oncoid and peloid grainstone facies. As such, archaeocyathan reefal bioconstructions represent a specific and limited locus of skeletal carbonate production and deposition. Consistent with data from coeval, globally dispersed lower Cambrian successions, our analysis of the Pedroche Formation supports the view that lower Cambrian carbonates have more in common with earlier, Neoproterozoic deposits than with younger carbonates dominated by skeletal production and accumulation. © 2013 Elsevier B.V.Jessica R. Creveling, David Fernández-Remolar, Marta Rodríguez-Martínez, Silvia Menéndez, Kristin D. Bergmann, Benjamin C. Gill, John Abelson, Ricardo Amils, Bethany L. Ehlmann, Diego C. García-Bellido, John P. Grotzinger, Christian Hallmann, Kathryn M. Stack, Andrew H. Knol

    An Enzyme Cascade for Selective Modification of Tyrosine Residues in Structurally Diverse Peptides and Proteins.

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    Bioorthogonal chemistry enables a specific moiety in a complex biomolecule to be selectively modified in the presence of many reactive functional groups and other cellular entities. Such selectivity has become indispensable in biology, enabling biomolecules to be derivatized, conjugated, labeled, or immobilized for imaging, biochemical assays, or therapeutic applications. Methyltransferase enzymes (MTase) that accept analogues of the cofactor <i>S</i>-adenosyl methionine have been widely deployed for alkyl-diversification and bioorthogonal labeling. However, MTases typically possess tight substrate specificity. Here we introduce a more flexible methodology for selective derivatization of phenolic moieties in complex biomolecules. Our approach relies on the tandem enzymatic reaction of a fungal tyrosinase and the mammalian catechol-<i>O</i>-methyltransferase (COMT), which can effect the sequential hydroxylation of the phenolic group to give an intermediate catechol moiety that is subsequently <i>O</i>-alkylated. When used in this combination, the alkoxylation is highly selective for tyrosine residues in peptides and proteins, yet remarkably tolerant to changes in the peptide sequence. Tyrosinase–COMT are shown to provide highly versatile and regioselective modification of a diverse range of substrates including peptide antitumor agents, hormones, cyclic peptide antibiotics, and model proteins
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