Ethnobotanical review of wild edible plants in Spain

This paper compiles and evaluates the ethnobotanical data currently available on wild plants traditionally used for human consumption in Spain. Forty-six ethnobotanical and ethnographical sources from Spain were reviewed, together with some original unpublished field data from several Spanish provinces. A total of 419 plant species belonging to 67 families was recorded. A list of species, plant parts used, localization and method of consumption, and harvesting time is presented. Of the seven different food categories considered, green vegetables were the largest group, followed by plants used to prepare beverages, wild fruits, and plants used for seasoning, sweets, preservatives, and other uses. Important species according to the number of reports include: Foeniculum vulgare , Rorippa nasturtium-aquaticum , Origanum vulgare , Rubus ulmifolius , Silene vulgaris , Asparagus acutifolius , and Scolymus hispanicus . We studied data on the botanical families to which the plants in the different categories belonged, overlapping between groups and distribution of uses of the different species. Many wild food plants have also been used for medicinal purposes and some are considered to be poisonous. This review highlights the rich traditional knowledge on edible plants that has remained in rural Spain. Until recently, many wild plants were used as dietary supplements. However, most of this knowledge survives only in the memory of the elderly, and will probably disappear in a few decades.  © 2006 The Linnean Society of London, Botanical Journal of the Linnean Society , 2006, 152 , 27–71.     

Expression of bovine lung prostaglandin F synthase in Escherichia coli

The full-length bovine lung prostaglandin(PG) F synthase cDNA was constructed from partial cDNA clones and ligated into bacterial expression vector pUC8 to develop expression plasmid pUCPF1. This plasmid permitted the synthesis of bovine lung PGF synthase in Escherichia coli. The recombinant bacteria overproduced a 36-KDa protein that was recognized by anti-PGF synthase antibody, and the expressed protein was purified to apparent homogeneity. The expressed protein reduced not only carbonyl compounds including PGD2 and phenanthrenequinone but also PGH2; and the Km values for phenanthrenequinone, PGD2, and PGH2 of the expressed protein were 0.1, 100, and 8 microM, respectively, which are the same as those of the bovine lung PGF synthase. The protein produced PGF2 alpha from PGH2, and 9 alpha, 11 beta-PGF2 from PGD2 at different active sites. Moreover, the structure of the purified protein from Escherichia coli was essentially identical to that of the native enzyme in terms of C-terminal sequence, sulfhydryl groups, and CD spectra except that the nine amino acids provided by the lac Z' gene of the vector were fused to the N-terminus. These results indicate that the expressed protein is essentially identical to bovine lung PGF synthase. We confirmed that PGF synthase is a dual function enzyme catalyzing the reduction of PGH2 and PGD2 on a single enzyme and that it has one binding site for NADPH.