Dielectric and optical properties of europium oxide films

The dielectric properties of vacuum-deposited europium oxide films have been investigated in the frequency range from 1 kHz to 1 MHz at various temperatures (300-543 K). The dielectric constant is found to depend on film thickness and it attains a constant value beyond 1000 Å. Films deposited at higher substrate temperatures (above 423 K) exhibit improved dielectric properties owing to the recovery of stoichiometry. The frequency variation of the loss factor exhibits a minimum which increases with rise in temperature. The breakdown field strength (about 106V cm-1) is found to be thickness dependent and it varies in accordance with the Forlani-Minnaja relation. The films exhibit ohmic conduction with an activation energy of 0.86 eV at low electric fields but at higher fields the conductivity becomes space charge limited. X-ray studies show that the films are amorphous in nature. The a.c. conductivity is proportional to ω at low frequency, whereas a square law dependence is observed at higher frequencies. The optical constants n, α and k and optical band gap are calculated from the UV-visible-near-IR spectra.

A new isoform of anti-lipopolysaccharide factor identified from the blue swimmer crab, Portunus pelagicus: Molecular characteristics and phylogeny

Anti-lipopolysaccharide factors are small proteins that bind and neutralize lipopolysaccharide and exhibit potent antimicrobial activities. This study presents the molecular characterization and phylogenetic analysis of the first ALF isoform (Pp-ALF1; JQ745295) identified from the hemocytes of Portunus pelagicus. The full length cDNA of Pp-ALF1 consisted of 880 base pairs encoding 293 amino acids with an ORF of 123 amino acids and contains a putative signal peptide of 24 amino acids. Pp-ALF1 possessed a predicted molecular weight (MW) of 13.86 kDa and theoretical isoelectric point (pI) of 8.49. Two highly conserved cysteine residues and putative LPS binding domain were observed in Pp-ALF1. Peptide model of Pp-ALF1 consisted of two α-helices crowded against a four-strand β-sheet. Comparison of amino acid sequences and neighbor joining tree showed that Pp-ALF1 has a maximum similarity (46%) to ALF present in Portunus trituberculatus followed by 39% similarity to ALF of Eriocheir sinensis and 38% similarity to ALFs of Scylla paramamosain and Scylla serrata. Pp-ALF1 is found to be a new isoform of ALF family and its characteristic similarity with other known ALFs signifies its role in protection against invading pathogens.