CdS thin films are grown by photochemical deposition from an aqueous solution and characterized by x-ray diffraction (XRD), Raman spectroscopy, photoluminescence measurement, and optical transmission spectroscopy. The films are deposited at room temperature and annealed at temperatures up to 500 °C. The as-deposited film is dominantly zinc blende cubic. The cubic phase remains dominant until the annealing temperature becomes higher than 400 °C. By the annealing at 450 °C, the XRD pattern turns to that of hexagonal phase. Moreover, its peak width decreases and the near-band-edge luminescence begins to be observed. The band gap is decreased by annealing below 400 °C and then abruptly increased by the annealing at 450 °C. This annealing behavior of the band gap is interpreted considering the quantum size effects, the band tail due to disorder, and the cubic-hexagonal transition.

CdS films were successfully formed on a glass substrate in an aqueous solution containing S2O3 2- and Cd2+ ions by photochemical reaction. S2O3 2- ions in the growth solution absorb ultra-violet light of wavelengths shorter than about 300 nm, and the excited S2O3 2- ions supply sulfur atoms and electrons to the metal ions such as Cd2+. Thus, the formation reaction of the sulfide semiconductor occurs in the only illuminated region. Photochemically deposited CdS thin films were polycrystalline of hexagonal structure. The composition of the films became stoichiometric by the annealing at temperatures higher than 300° C.

The relationship between sulfation and polymerization in chondroitin sulfate (CS) biosynthesis has been poorly understood. In this study, we investigated the specificity of bovine serum UDP-GalNAc: CS beta-GalNAc transferase responsible for chain elongation using structurally defined acceptor substrates. They consisted of tetra- and hexasaccharide-serines that were chemically synthesized and various regular oligosaccharides with a GlcA residue at the nonreducing terminus, prepared from chondroitin and CS using testicular hyaluronidase. The enzyme preparation was obtained from fetal bovine serum by means of heparin-Sepharose affinity chromatography. The preparation did not contain the alpha-GalNAc transferase recently demonstrated in fetal bovine serum (Kitagawa et al., J. Biol. Chem., 270, 22190-22195, 1995), that utilizes common acceptor substrates. The beta-GalNAc transferase used as acceptors, two hexasaccharide-serines GlcA beta 1-3GalNAc beta 1-4GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser and GlcA beta 1-3GalNAc(4-sulfate) beta 1-4GlcA beta 1-3Gal (4-sulfate) beta 1-3Gal beta 1-4Xyl beta 1-O-Ser, but neither the monosulfated hexasaccharide-serine GlcA beta 1-3GalNAc(4-sulfate) beta 1-4GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser nor tetrasaccharide-serines with or without a sulfate group at C-4 of the third sugar residue Gal-3 from the reducing end. The results indicated that the sulfate group at the Gal-3 C-4 markedly affected the transfer of GalNAc to the terminal GlcA. In addition, a sulfate group at C-4 of the reducing terminal GalNAc of regular tetrasaccharides remarkably enhanced the GalNAc transfer, suggesting that the enzyme recognizes up to the fourth saccharide residue from the nonreducing end. The level of incorporation into a tetra- or hexasaccharide containing a terminal 2-O-sulfated GlcA residue was significant, whereas there was no apparent incorporation into tetra- or hexasaccharides containing a terminal 3-O-sulfated GlcA or penultimate 4,6-O-disulfated GalNAc residue. These results indicated that sulfation reactions play important roles in chain elongation and termination.

No abstract

No abstract

Edited by Judit OvádiKeywords: GFAT1 Crystal structure Sugar-phosphate isomerization Substrate-binding a b s t r a c t Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes.

During the course of a study to elucidate the role of modification of the common polysaccharide-protein linkage structure, GlcA␤1-3Gal␤1-3Gal␤1-4Xyl␤1-O-Ser, in biosynthetic sorting mechanisms of the different sulfated glycosaminoglycan chains, a novel N-acetylgalactosamine (GalNAc) transferase was discovered in fetal bovine serum. The enzyme catalyzed the transfer of

No abstract