The Raman data for T1NO, (mp 206°C) in the pure molten state are: 1036 (10, p), 1328 (3.3, dp), 1383 (3.9, dp), and 1637 (2.S) cm-I , and two relatively low frequencies, 708 (1.3) and 813 (1.7) em-I. The results a;e examined in light of the vibrational assignments for D3h and C2V point group symmetries in solid-state mtrates, and for D3h symmetry for related nitrates in the molten state. An assignment of the Raman activity of molten T1N03 based on retention of D3h symmetry is advanced; the appearance of the Raman "forbidden" frequencies (V2) and the loss of degeneracy (V3) are attributed to cationic environmental effects in this molten salt.
Recent subcellular fractionation studies have raised the possibility that Na+-K+-ATPase might be present in both the apical and the basal-lateral membranes of exocrine gland acinar cells. Analytical fractionation and immunofluorescence microscopy studies of rat parotid glands were performed to confirm this interpretation. The distributions of biochemical markers after analyses based on differential sedimentation, equilibrium density-gradient centrifugation, and partitioning in an aqueous polymer two-phase system defined a total of 15 physically and biochemically distinct membrane populations. Among these populations, it was possible to select one (designated population i) with the characteristics expected of acinar cell basal-lateral plasma membranes. It contained Na+-K+-ATPase enriched 33-fold, and gamma-glutamyl transpeptidase enriched 23-fold with respect to the initial homogenate. A second population (designated population c) had the characteristics expected of acinar cell apical plasma membranes; it contained Na+-K+-ATPase enriched 28-fold, and gamma-glutamyl transpeptidase enriched 53-fold with respect to the initial homogenate. Although the identification of population c remains provisional, immunofluorescence studies verified that Na+-K+-ATPase is present in both the apical and the basal-lateral acinar cell plasma membranes. In view of these results, it is likely that the apical Na+-K+-ATPase would participate in series with basal-lateral sodium- and chloride-entry pathways in driving the secretory electrolyte fluxes.
a s 9 1o0,982 NA. -P_366 NA 2. --APPARENT (SEE TEXTI STRUCTURAL EFFEGT ) unless CC License in place (see abstract). ecsdl.org/site/terms_use address. Redistribution subject to ECS terms of use (see 35.8.11.2 Downloaded on 2015-06-17 to IP ) unless CC License in place (see abstract). ecsdl.org/site/terms_use address. Redistribution subject to ECS terms of use (see 35.8.11.2 Downloaded on 2015-06-17 to IP
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.