Hazard screening of chemical releases and environmental equity analysis of populations proximate to toxic release inventory facilities in Oregon.

A comprehensive approach using hazard screening, demographic analysis, and a geographic information system (GIS) for mapping is employed to address environmental equity issues in Oregon. A media-specific chronic toxicity index [or chronic index (CI)] was used to compare environmental chemical releases reported in the EPA's Toxic Chemical Release Inventory (TRI) database. In 1992, 254 facilities reportedly released more than 40 million pounds of toxic chemicals directly into the environment on-site or transferred them to sewage treatment plants or other off-site facilities for disposal and recycling. For each reported on-site TRI chemical release, a CI based on oral toxicity factors and total mass was calculated. CIs were aggregated on a media-, facility-, and chemical-specific basis. Glycol ethers, nickel, trichloroethylene, chloroform, and manganese were ranked as the top five chemicals released statewide based on total CI. In contrast, based on total mass, methanol, nickel, ammonia, acetone, and toluene were identified as the top five TRI chemicals released in Oregon. TRI facility rankings were related to the demographics and household income of surrounding neighborhoods using bivariate GIS mapping and statistical analysis. TRI facilities were disproportionately located in racial and ethnic minority neighborhoods. They were also located in areas with lower incomes compared to those in the surrounding county. No relationship was observed between the hazard ranking of the TRI facilities overall and socioeconomic characteristics of the community in which they were located.

Calmodulin-dependent protein kinase and associated substrates in Torpedo electric organ.

Calcium plus calmodulin (Ca2+/CaM)-dependent protein kinase activity was demonstrated in subcellular fractions from Torpedo californica electric organ. A protein kinase activity dependent on Ca2+/CaM was purified about 200-fold from electric organ cytosol using DEAE-cellulose and CaM-affinity chromatography. The most effective exogenous substrates for this enzyme were the synapse-specific protein Synapsin I (Protein I) and histone f3. Phosphorylase b, skeletal muscle myosin light chains, casein, phosvitin, histone f2b, and G-substrate were relatively poorly phosphorylated by Torpedo CaM-protein kinase. Thus, the enzyme differs in its substrate specificity from known cyclic nucleotide-dependent protein kinases, myosin light chain kinase and phosphorylase kinase. The Km for ATP was 15-20 microM; for Synapsin I, 0.8 microM; and for CaM, 85 nM. Two major endogenous substrates (Mr = 62,000 and 54,000) for CaM-protein kinase co-purified with the enzyme through the CaM-affinity column step. These two substrates, as well as the enzyme, were present in other subcellular fractions in addition to the cytosol, including crude membranes and purified synaptic vesicles. A third major substrate (Mr = 39,000) could be separated from the enzyme during purification and appeared to be localized primarily in the cytosol. CaM-protein kinase increased the phosphorylation of both serine and threonine residues in endogenous substrates. In contrast to previous reports, no evidence for Ca2+/CaM-dependent phosphorylation of any subunit of the acetylcholine receptor was obtained.