Pliocene and Pleistocene sediments from Sulu Sea ODP Sites 768 and 769 contain high-resolution records of pelagic sedimentation in a deep marine silled basin. Carbonate analyses reveal that both sites are free of pelagic carbonate up until 2.4 Ma, at which time carbonate becomes a major component of the pelagic marl sedimentation. The timing of this increase in calcium carbonate accumulation is...

Various concentrations of anionic surfactant, sodium dodecyl sulfate (SDS), were used to control the growth of calcium carbonate crystals. The obtained calcium carbonate particles were characterized by Fourier transform infrared spectrometry (FT-IR), X-ray diffraction (XRD), field emission-scanning electron microscopy (FE-SEM), laser scattering particle size analyzer and zeta potential analyzer...

The present paper compiles an up-to-date taxonomic inventory of dasycladalean green algae of the KimmeridgianEarly Berriasian Plassen Carbonate Platform and their resediments in basinal sediments (e.g., Barmstein Limestone, Sillenkopf Formation) of the Northern Calcareous Alps of Austria (p.p. Germany). Today, the Plassen Carbonate Platform sensu lato (or Plassen Group) is divided into three in...

Controlling the growth of the polymorphs of calcium carbonate is important in understanding the changing environmental conditions in the oceans. Aragonite is the main polymorph in the inner shells of marine organisms, and can be readily converted to calcite, which is the most stable polymorph of calcium carbonate. Both of these polymorphs are significantly more stable than vaterite, which is th...

Calcium carbonate is the material that builds up the spicules of the calcareous sponges. Recent results revealed that the calcium carbonate/biocalcite-based spicular skeleton of these animals is formed through an enzymatic mechanism, such as the skeleton of the siliceous sponges, evolutionarily the oldest animals that consist of biosilica. The enzyme that mediates the calcium carbonate depositi...

The complexation of Cm(III) with the recombinant N-lobe of human serum transferrin (hTf/2N) is investigated in the pH range from 4.0 to 11.0 using TRLFS. At pH ≥ 7.4 a Cm(III) hTf/2N species is formed with Cm(III) bound at the Fe(III) binding site. The results are compared with Cm(III) transferrin interaction at the C-lobe and indicate the similarity of the coordination environment of the C- an...