12 research outputs found
The role of reactive center loop in serpin inhibitory mechanism.
The role of reactive center loop in serpin inhibitory mechanism
Conformational Equilibrium of the Reactive Center Loop of Antithrombin Examined by Steady State and Time-Resolved Fluorescence Measurements: Consequences for the Mechanism of Factor Xa Inhibition by Antithrombin−Heparin Complexes †
Nattokinase (Bac s 1), a subtilisin family serine protease, is a novel allergen contained in the traditional Japanese fermented food natto
Background: Immediate allergy caused by natto, a popular Japanese food prepared by fermenting soybeans with Bacillus subtilis var. natto, has been reported. Polygamma glutamic acid (PGA) in the sticky substance around natto beans has been reported to be a causative allergen of natto allergy. However, some of our patients with natto allergy were negative for PGA in the skin prick test (SPT). The sticky substance of natto beans contains a subtilisin family serine protease, nattokinase, along with PGA. In this study, we aimed to examine the antigenicity of nattokinase in natto allergy. Methods: Eight patients, who developed symptoms after ingesting natto and positively reacted to natto (seven to the sticky substance in natto and one to the whole natto product) in their SPT, were enrolled in this study. To analyze IgE reactivity, we performed immunoblotting, ELISA, and SPT for natto (bean and sticky substance), and/or PGA, and/or nattokinase and/or cultured B. subtilis var. natto extract. Results: In the SPT, four cases each were PGA-positive and PGA-negative. Immunoblotting of the sera from PGA-negative patients showed a protein band at 30 kDa, which was identified as nattokinase. Three PGA-negative cases, but not three PGA-positive cases, showed a positive reaction to nattokinase in the SPT and had a history of atopic dermatitis. The ELISA for nattokinase revealed a positive reaction of PGA-negative cases and negative reaction of PGA-positive cases in the SPT. Conclusions: We identified a subtilisin family serine protease, nattokinase, as a novel allergen in natto allergy patients unsensitized to PGA
Change in Environment of the P1 Side Chain upon Progression from the Michaelis Complex to the Covalent Serpin−Proteinase Complex †
Construction of a potato fraction library for the investigation of functional secondary metabolites
Productivity and bioactivities of antimicrobial metabolites, enokipodins A-D, produced in Flammulina velutipes and F. rossica
Reverse phase protein microarray for identification of IL6 receptor ligation-induced insulin receptor, PI3K/AKT, and JAK/STAT signaling pathways in the CARD11 mutated lymphoma cell line OCI-Ly3.
Productivity and bioactivity of enokipodins A–D of Flammulina rossica and Flammulina velutipes
Enokipodins are antimicrobial sesquiterpenes produced by Flammulina velutipes in a mycelial culture medium. To date, enokipodin production has not been reported in other members of the genus Flammulina. Hence, in this study, the production of enokipodins A, B, C, and D by F. velutipes and F. rossica was investigated. Some strains of F. rossica were confirmed to produce at least one of the four enokipodins in the culture medium. However, some strains of F. velutipes did not produce any of the enokipodins. In an antibacterial assay using liquid medium, enokipodin B showed the strongest growth inhibitory activity against Bacillus subtilis among the four types of enokipodins. Enokipodin B inhibited the spore germination of some plant pathogenic fungi. Enokipodins B and D exerted moderate anti-proliferative activity against some cancer cell lines, and enokipodins A and C inhibited the proliferation of the malarial parasite, Plasmodium falciparum. © 2020, © 2020 Japan Society for Bioscience, Biotechnology, and Agrochemistry