Biodegradation of chlorinated ethenes by a methane-utilizing mixed culture.

Chlorinated ethenes are toxic substances which are widely distributed groundwater contaminants and are persistent in the subsurface environment. Reports on the biodegradation of these compounds under anaerobic conditions which might occur naturally in groundwater show that these substances degrade very slowly, if at all. Previous attempts to degrade chlorinated ethenes aerobically have produced conflicting results. A mixed culture containing methane-utilizing bacteria was obtained by methane enrichment of a sediment sample. Biodegradation experiments carried out in sealed culture bottles with radioactively labeled trichloroethylene (TCE) showed that approximately half of the radioactive carbon had been converted to 14CO2 and bacterial biomass. In addition to TCE, vinyl chloride and vinylidene chloride could be degraded to products which are not volatile chlorinated substances and are therefore likely to be further degraded to CO2. Two other chlorinated ethenes, cis and trans-1,2-dichloroethylene, were shown to degrade to chlorinated products, which appeared to degrade further. A sixth chlorinated ethene, tetrachloroethylene, was not degraded by the methane-utilizing culture under these conditions. The biodegradation of TCE was inhibited by acetylene, a specific inhibitor of methane oxidation by methanotrophs. This observation supported the hypothesis that a methanotroph is responsible for the observed biodegradations.

Glycoprotein reutilization in regenerating microvilli after renal ischemia in rats.

Renal ischemia causes a reversible loss of microvillar membrane (MVM) of the proximal tubule cell and of MVM enzyme specific activities (S.A.). We sought to determine if recovery of the MVM glycoprotein was accomplished through de novo synthesis or recycling. Renal ischemia (25 min) was induced in rats by occlusion of the left renal artery, followed by 15 min or 4 hrs of reflow of blood. Radiolabelled fucose was injected into rats before or after ischemia and was used as a marker for new glycoprotein synthesis or recycling of prelabelled glycoprotein. Ischemia, followed by 15 min of reflow, caused a 49% reduction in protein associated with the isolated MVM fraction of the ischemic kidney. There was also a decrease in newly fucosylated glycoprotein in both homogenate and MVM fraction measured as S.A. or total amount of labeled glycoprotein. Pre-labelled glycoproteins had no change in S.A. in homogenates or MVM fractions of ischemic or contralateral kidneys. However, the total amount of labeled glycoprotein in the ischemic MVM fraction was reduced. At 4 hrs of reflow, protein content of the MVM fraction was back to normal. Pre-labelled glycoproteins of the ischemic homogenate and MVM fraction were also back to normal with no significant dilution of glycoprotein S.A. by newly synthesized protein, indicating that glycoprotein recycling occurs to a large extent in the ischemic kidney.