Movement and metabolism of S-benzyl O,O-diisopropyl phosphorothiolate (Kitazin P) and O-ethyl S,S-diphenyl phosphorodithiolate (edifenphos) in various types of soils.

Movement and Metabolism of 32P and 35S-double labeled Kitazin P (S-benzyl O,O-diisopropyl phosphorothiolate) and 35S-labeled edifenphos (O-ethyl S,S-diphenyl phosphorodithiolate) were examined with three types of soils, sandy loam, alluvial clay loam, and volcanic ash loam. Vertical movement of both the compounds in soil column was different with soil types, and the order of mobility in soil column was as follows: sandy loam greater than alluvial clay loam greater than volcanic ash loam. Persistence of edifenphos in soil was shorter than that of Kitazin P. Main degradation products at the initial stage of metabolism were S,S,S-triphenyl phosphorotrithiolate, O,O-diethyl S-phenyl phosphorothiolate, S-phenyl dihydrogen phosphorothiolate and diphenyl disulfide in edifenphos and O,O-diisopropyl hydorgen phosphorothioate in Kitazin P. Sulfur atom of Kitazin P was found in sulfuric acid at a minor level through dibenzyl disulfide and toluene-alpha-sulfonic acid, and that of edifenphos was converted to sulfuric acid through diphenyl disulfide and benzenesulfonic acid. Kitazin P under flooded condition of alluvial clay loam was slightly more persistent as compared with upland condition. Sterilized condition of Kitazin P did not cause any appreciable degradation throughout the experimental period, but such condition did not necessarily prevent the degradation of edifenphos.

Characteristics of membrane-bound and free hepatic ribosomes from insulin-deficient rats. I. Acute experimental diabetes mellitus.

Membrane-bound and free ribosomes were prepared by discontinuous density gradient centrifugation from livers of rats 2-3 days after receiving alloxan (75 mg/kg) or streptozotocin (100 mg/kg). Hepatocytes from these animals were also examined by electron microscopy and subjected to quantitative morphometric analysis. The results indicated that the two populations of hepatic ribosomes respond differently to acute insulin deficiency. There was an overall reduction (P < 0.001) in total number of bound ribosomes per volume cytoplasm: the remaining bound ribosomes underwent a shift to smaller-sized ribosomal messenger RNA (mRNA) aggregates (P < 0.02); and the proteinsynthetic activity of these bound ribosomes was less than normal (P < 0.02) when protein synthesis was directed by endogenous mRNA. However, there was no difference between bound ribosomes from livers of normal and diabetic rats when protein synthesis was directed by polyuridylic acid. In contrast, free ribosomes were unchanged in number and degree of ribosomal mRNA aggregation, but displayed a significantly increased rate of in vitro protein synthesis (P < 0.01) as compared to normal controls. This increased protein-synthetic activity occurred when amino acid incorporation was directed by endogenous mRNA or polyuridylic acid. These changes in structure and function of bound and free hepatic ribosomes were prevented by the concomitant administration of insulin. The decrease in protein-synthetic activity of bound hepatic ribosomes from acutely diabetic rats seems to be secondary to marked disruption and disaggregation of the rough endoplasmic reticulum (RER) with production of smaller ribosomal mRNA aggregates which incorporate less amino acids into protein. Increased protein synthetic activity of free ribosome appears to be related to the ability of these ribosomes to copy mRNA more efficiently.