Ozone stress modulates amine oxidase and lipoxygenase expression in lentil (Lens culinaris) seedlings.

The effect of ozone stress on polyamine metabolism and membrane lipid peroxidation in lentil seedlings through the amine oxidase and lipoxygenase activity and expression has been investigated. Ozone is shown to control the expression of these enzymes at the transcriptional level, down-regulating the amine oxidase gene and up-regulating the lipoxygenase gene. The decrease of amine oxidase activity correlated with the increase of putrescine concentration in the ozone-treated plantlets, whereas the increase of lipoxygenase activity was paralleled by enhanced membrane lipid peroxidation.

The Asn-linked carbohydrate chains of human Tamm-Horsfall glycoprotein of one male. Novel sulfated and novel N-acetylgalactosamine-containing N-linked carbohydrate chains.

Human Tamm-Horsfall glycoprotein has been purified from the urine of one male. The Asn-linked carbohydrate chains were enzymically released by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F, and separated from the remaining protein by gel-permeation chromatography on Bio-Gel P-100. Fractionation of the intact (sulfated) sialylated carbohydrate chains was achieved by a combination of three liquid-chromatographic techniques, namely, anion-exchange FPLC on Q-Sepharose, amine-adsorption HPLC on Lichrospher-NH2, and high-pH anion-exchange chromatography on CarboPac PA1.

Structures of fifteen oligosaccharides isolated from new-born meconium.

New born meconium contains at least a hundred oligosaccharides. In this study the isolation and characterization of the major constituents is described. The structure elucidation of 15 neutral and acidic oligosaccharides was carried out by methylation analysis, mass spectrometry and 360-MHz 1H-NMR spectroscopy.

Structure determination by 360-MHz 1H-NMR spectroscopy and methylation analysis of a biantennary glycan of the N-acetyllactosaminic type isolated from rat-liver plasma membrane.

Glycopeptides obtained by exhaustive pronase digestion of delipidated rat liver plasmic membranes were purified by gel filtration on Sephadex G-25. These glycopeptides were further fractionated by affinity chromatography on a concanavalin-A--Sepharose 4B column into the following fractions: (a) glycopeptides which did not bind to the column (fraction 1); (b) glycopeptides with weak affinity for concanavalin-A--Sepharose, which could be eluted with buffer only (fraction 2); (c) glycopeptides retained on the column and which could be eluted specifically with buffer containing 0.2 M methyl alpha-glucoside (fraction 3).