Removal of heavy metals in an abandoned mine drainage via ozone oxidation: a pilot-scale operation.

The objective of this study was to evaluate the ozone oxidation of dissolved heavy metals in an abandoned mine drainage (AMD) by conducting a pilot-scale operation at two different ozone doses of 7.5 and 24.0 g O(3)/h into an ozone reactor. A portion of the abandoned mine drainage near the Jungam Mine in Samchuck, Korea was pumped into this pilot-scale plant and used as an influent for the ozone oxidation. Some possible precipitates of metal oxides and hydroxides that resulted from the pilot-scale ozone oxidation of the dissolved Fe and Mn ions in the AMD (with a hydraulic retention time of 106 seconds in the ozone reactor) were effectively removed via sand filtration. A six-hour ozone oxidation with an ozone dose of 24.0 g O(3)/h and subsequent sand filtration, before backwashing the sand filter bed, can meet Korean drinking water quality standards (less than 0.3 mg/L) for Fe and Mn in the sand filter effluent under the operating conditions that were used in this study. The SO(4)(-2) concentrations and alkalinities of the influents were not affected by the ozone oxidation. The pH values of the influents were neutral or slightly alkaline, and after the six-hour oxidation, increased very slightly. These experiment results show that the ozone oxidation of dissolved heavy metals and the subsequent sand filtration of metal precipitates are desirable alternatives to removing heavy metals in an abandoned mine drainage.

Identification, expression, and nuclear location of murine Mage-b2 protein, a tumor-associated antigen.

MAGE-1, which was originally identified by reacting with cytolytic T lymphocytes derived from the blood of melanoma patients, is a member of a gene family consisting of 17 structurally related genes. The MAGE genes are expressed only in the testis among normal tissues and in a number of human tumors of various histological types. Murine MAGE (also called SMAGE or Mage) genes were found in a study aimed at detecting mouse genes homologous to human MAGE genes. However, the biological functions of MAGE and Mage are currently unknown. To understand the biological functions of Mage, in the present study a recombinant SMAGE2 (Mage-b2) protein of 43 kDa was produced and monoclonal antibodies reactive with Mage-b2 protein were generated. One monoclonal antibody, smpG4A, specifically recognized a 43 kDa protein in lysates of Mage-b2 mRNA-positive sarcoma cells and of the testis. Immunohistochemistry showed that Mage-b2 is located in the nucleus of Mage-b2 mRNA-positive sarcoma cells. These results should contribute to understanding the biological functions of Mage.