Search results for "Plant Biochemistry"
showing 3 items of 13 documents
How subtle is the "terroir" effect? Chemistry-related signatures of two "climats de Bourgogne".
2014
The chemical composition of grape berries is influenced by various environmental conditions often considered to be representative of a "terroir". If grapes from a given terroir are assumed to reflect this origin in their chemical compositions, the corresponding wine should also reflect it. The aim of this work was therefore to reveal the "terroir" expression within the chemodiversity of grapes and related wines, using ultrahigh-resolution mass spectrometry. Grapes and corresponding wines, from two distinct - though very proximate - terroirs of Burgundy were analyzed over three vintages (2010, 2011 and 2012). Ultrahigh-resolution mass spectrometry and ultra-high performan…
Sex ratio and spatial distribution of male and female Antennaria dioica (Asteraceae) plants
2011
Sex ratio, sex spatial distribution and sexual dimorphism in reproduction and arbuscular mycorrhizal colonisation were investigated in the dioecious clonal plant Antennaria dioica (Asteraceae). Plants were monitored for five consecutive years in six study plots in Oulanka, northern Finland. Sex ratio, spatial distribution of sexes, flowering frequency, number of floral shoots and the number and weight of inflorescences were recorded. In addition, intensity of mycorrhizal fungi in the roots was assessed. Both sexes flowered each year with a similar frequency, but the overall genet sex ratio was strongly female-biased. The bivariate Ripley’s analysis of the sex distribution showed that within…
The influence of α-aminophosphonic acids on the activity of aminopeptidase from barley seeds—an approach to determine the enzyme specificity
2015
Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds (Hordeum vulgare L.) metallo-aminopeptidase have been determined to evaluate structural requirements of this enzyme. The enzyme was sensitive mostly to the influence of phosphonic acid analogues of phenylalanine and its homologues, thus showing narrow specificity if compared with porcine aminopeptidases M1 and M17 and with Plasmodium aminopeptidase M17.