Functional characterization of Longepsin involved in hemoglobin digestion from the Haemaphysalis longicomis(Contributed Paper,Proceedings of the 53rd Annual Meeting of Northern Region) (original) (raw)
Japanese journal of applied entomology and zoology, 1995
An anti-microbial substance in the mandibular gland of L. fuliginosus was identified as 3-formyl-7, 11dimethyl-(2E, 6Z, 10)-dodecatrien-l-al. This substance inhibited the germination of spores of plant pathogens such as Colletotrichum lagenarium, Fusarium oxysporum SCHLECHTENDAHL, Gibberella fujikuroi SAW. WR., Pestulotia longiseta, Pyricularia oryzae CAVARA, Verticillum dahliae, and of insect pathogens such as Metarhizium anisopliae F126, Beauveria bassiana F18, Paecilomyces fumosoroseus 522, Verticillium lecanii F126. Moreover, it also inhibited the growth of gram positive and gram negative bacteria. Comparison with dendrolasin, farnesal, and farnesol suggested that the structure of the dialdehyde double bond contributes to the antimicrobial activity.
Activation Mechanism of Receptors on the Biomembrane
Maku, 2009
The biological importance of membrane protein is emphasized in statistical analyses of the genomes that indicate about 30% of all open reading frames encode membrane proteins. For the purpose of performing structural biology on membrane proteins, we have been developing a methodology for chemical synthesis of membrane proteins. Now, accumulated knowledge and experience has enabled us to work on the structure and function of transmembrane-juxtamembrane region of membrane protein with solid state NMR and other spectroscopic techniques. Since little attention has been paid to this portion of protein as such, obtaining the structural information that provides a clue to fully understand how membrane protein, especially, receptor on the membrane, passes the structural change at the outside to the inside. In this review, we introduce our approach from peptide chemistry to work on structural biology of membrane protein.