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Arabinogalactan proteins (AGPs) encompass a diverse group of plant cell wall proteoglycans, which play an essential role in plant development, signaling, plant‐microbe interactions, and many others. Although they are widely distributed throughout the plant kingdom and extensively studied, they remain largely unexplored in the lower plants, especially in seaweeds. Ulva species have high economic potential since various applications were previously described including bioremediation, biofuel production, and as a source of bioactive compounds. This article presents the first experimental confirmation of AGP‐like glycoproteins in Ulva species and provides a simple extraction protocol of Ulva lactuca AGP‐like glycoproteins, their partial characterization and unique comparison to scarcely described Solanum lycopersicum AGPs. The reactivity with primary anti‐AGP antibodies as well as Yariv reagent showed a great variety between Ulva lactuca and Solanum lycopersicum AGP‐like glycoproteins. While the amino acid analysis of the AGP‐like glycoproteins purified by the β‐d‐glucosyl Yariv reagent showed a similarity between algal and land plant AGP‐like glycoproteins, neutral saccharide analysis revealed unique glycosylation of the Ulva lactuca AGP‐like glycoproteins. Surprisingly, arabinose and galactose were not the most prevalent monosaccharides and the most outstanding was the presence of 3‐O‐methyl‐hexose, which has never been described in the AGPs. The exceptional structure of the Ulva lactuca AGP‐like glycoproteins implies a specialized adaptation to the marine environment and might bring new insight into the evolution of the plant cell wall.

This paper deals with the physico-chemical properties of ethanol and ethanol-water solutions. The data of ethanol properties and its water solutions, which were obtained from literature, are presented in the form of Equations and Tables.Extended properties include data for pure ethanol (density, vapor pressure, surface tension, viscosity, molar and specific heat capacity, enthalpy of evaporation, thermal conductivity and static relative permittivity) and tabled data for ethanol-water solutions (0–100% ethanol) as well: concentrative properties, surface tension and thermal conductivity at20 °C, density, viscosity, boiling point and equilibrium liquid-vapor at normal pressure.

Many factors affect successful virus propagation and plant defence responses. Heat shock protein (Hsp) expression after heat shock plays an ambiguous role in viral infection. On the one hand, Hsp70 participates in plant defence response; on the other hand, Hsp70 could interact with viral proteins and facilitate virus propagation.• Here, we studied metabolic adaptations of Nicotiana tabacum L. subjected to heat shock (42°C, 2 h) before or after inoculating the plants with Potato virus Y (potyvirus). RT-qPCR and ELISA were used for potyvirus quantification. Hsp70 and Hsp90 isoforms were analysed by Western blotting. Salicylic, quinic and chlorogenic acid content was determined by LC-MS. The activity of Hatch-Slack enzymes (as markers of potyviral infection in tobacco) and glycosidases was assayed.• Application of heat shock before or after inoculation showed accelerated potyviral propagation in comparison with only inoculated plants. Plants exposed to heat shock and concurrently inoculated showed higher potyviral content, higher amount of Hsp70, together with late decline of quinic acid content and low chlorogenic acid content. Spread of potyviral infection correlated with enhanced salicylic acid content and activities of enzymes of the Hatch-Slack cycle, aand b-galactosidase, a-mannosidase, a-glucosidase and b-N-acetylhexosaminidase.• Heat shock proteins accelerate potyviral propagation. The lower weight cytosolic and mitochondrial Hsp70 (~50-75 kDa) persist throughout the viral infection. Also, the plant defense response results in increase of salicylic and chlorogenic acids but decrease of quinic acid content.

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