Search results for " Esterases"
showing 3 items of 3 documents
Specific inflammatory response of Anemonia sulcata (Cnidaria) after bacterial injection causes tissue reaction and enzymatic activity alteration
2015
The evolution of multicellular organisms was marked by adaptations to protect against pathogens. The mechanisms for discriminating the ’’self’’ from ’’non-self” have evolved into a long history of cellular and molecular strategies, from damage repair to the co-evolution of host-pathogen interactions. We investigated the inflammatory response in Anemonia sulcata (Cnidaria: Anthozoa) following injection of substances that varied in type and dimension, and observed clear, strong and specific reactions, especially after injection of Escherichia coli and Vibrio alginolyticus. Moreover, we analyzed enzymatic activity of protease, phosphatase and esterase, showing how the injection of different ba…
Study of molecular mechanisms of stress response in Oenococcus oeni and implementation of tools for the functional exploration of enological genes
2015
O. oeni is responsible for wine malolactic fermentation. As any organism, O. oeni tries to adapt its physiology to environmental fluctuations by producing Hsp proteins encoded by the hsp genes. In O. oeni, CtsR is currently the only regulator of hsp genes. As an alternative to the lack of genetic tool, with the goal of understanding the mechanisms of O. oeni stress response, we developed a new expression vector, the pSIPSYN, to produce antisense RNA targeting of hsp18 mRNA. The synthesis of hsp18 asRNA leads to the decrease in the protein level of Lo18 and induced a loss of cultivability after heat or acid shock showing for the first time in vivo involvement of Lo18 in thermotolerance and a…
Purification and reassessment of ligand binding by the recombinant, putative juvenile hormone receptor of the tobacco hornworm, Manduca sexta
1996
The 29 kDa protein from the larval epidermis of the tobacco hornworm, Manduca sexta, that specifically bound photoaffinity analogs of JH I and JH II was produced by a recombinant baculovirus (rJP29). The higher of the two molecular weight forms made corresponded to a protein that could be formed by read‐through of the TGA termination codon to the following TAA. The previously reported, apparent high affinity binding of [methyl‐3H]‐JH I by rJP29 as measured by the dextran‐coated charcoal (DCC) assay [Palli et al., Proc Natl Acad Sci USA 91:6191–6195 (1994)] was found to be artifactual due to endogenous cellular esterases that co‐purified with rJP29 through both DEAE cellulose and MonoQ chrom…