Uranium Sorption on “Tezontle” Volcanic Rock

It is described a study that demonstrates that hexavalent uranium ions were sorbed by the naturally occurring mineral using a batch technique. This mineral is found in abundant quantities in Mexico. Our study focused on the separation of UVI from synthetic aqueous systems of both H2O-UO2(NO3)2.6H2O (acid) and H2ONa4[ UO2(CO3)3] (basic). The chemical speciation was performed by using high voltage electrophoresis, and the uranium content was determined by UV-Vis Spectroscopy. The quantified U(VI) sorption by tezontle from acidic and basic systems was 2.72 and 1.68 μmol/g, respectively, and the sorption behavior is discussed considering the surface charge of the tezontle at different pH values based on the point of zero charge characteristic of this material.

No alpha-lactalbumin-like activity detected in a low molecular mass protein fraction of rat epididymal extract

The same low M(r) protein fraction of epididymal luminal fluid as that studied previously by Hamilton in 1981 was assayed for alpha-lactalbumin (alpha-lac) activity with bovine milk galactosyltransferase (GalTase) as the enzyme source and bovine serum albumin (BSA) to make the total protein concentrations of all the samples in each assay constant. No alpha-lac activity could be detected in this fraction. When glucose was used as an acceptor, radioactivity passing through the ion exchange column used to retain the remaining UDP-galactose did increase with the amount of the proteins of the low M(r) fraction, but this increase was observed not only for samples with an acceptor but also for samples without. The increased radioactive product co-migrated in high-voltage electrophoresis with galactose, not lactose. When GlcNAc was used as an acceptor, the situation was the same, and the increased radioactive product co-migrated with galactose, not LacNAc. No inhibition of bovine milk GalTase activity by the low M(r) proteins was observed. Addition of protein, either BSA or the low M(r) fraction of epididymal luminal fluid, to assay medium that contained no proteins other than GalTase enhanced the GalTase activity both in forming lactose in the presence of glucose and also LacNAc in the presence of GlcNAc. It appears that the earlier reports of alpha-lac-like activity in epididymal fluids and extracts may have been due to the presence of enzymes liberating free galactose from UDP-galactose and/or a stimulatory non-specific effect of the protein in the solutions on the lactose synthesis activity of the GalTase.

Creatine Kinase Isoforms: Investigation of Inhibitors of in Vitro Degradation and Establishment of a Reference Range

The in vitro stability of creatine kinase isoforms was examined by separation with high voltage electrophoresis. The effect of inhibitors of carboxypeptidase was evaluated. Preservation of samples is essential to inhibit in vitro changes in isoform pattern. EDTA at a final concentration of 15 mmol/L is recommended. Using appropriately preserved samples, normal reference intervals for the MM isoforms have been established.