Zobrazeno 1 - 10
of 160
pro vyhledávání: '"Kyoichi Kobashi"'
Publikováno v:
Biological and Pharmaceutical Bulletin. 30:11-14
A gene (astA) encoding arylsulfate sulfotransferase (ASST), which transfers a sulfate group from phenolic sulfate esters to phenolic acceptors, was cloned from a Eubacterium A-44 genomic library. The probe (1.5 kb fragment) for the astA gene was prep
Autor:
Hideo Ueda, Kyoichi Kobashi
Publikováno v:
Journal of Japan Association on Odor Environment. 36:270-274
Autor:
Teruaki Akao, Kiyoshi Kawabata, Yoko Sakashita, Erika Yanagisawa, Yoko Wakui, Kazuhisa Ishihara, Yasuharu Mizuhara, Kyoichi Kobashi
Publikováno v:
Journal of Pharmacy and Pharmacology. 52:1563-1568
When baicalin was orally administered to conventional rats, it was detected in their plasma for 24 h after administration, but baicalein, the aglycone of baicalin, was not detected. However, when baicalin was given to germ-free rats, only a small amo
Publikováno v:
Journal of Biochemistry. 125:27-30
A peptide has been isolated from pronase digest of bovine serum albumin as the stimulatory factor of streptolysin S (SLS) production by Streptococcus pyogenes, and its primary structure has been deduced [Akao et al. (1992) Infect. Immun. 60, 4777-478
Publikováno v:
Biological and Pharmaceutical Bulletin. 21:245-249
Enzyme immunoassay (EIA) for the determination of compound K (C-K), a major metabolite of ginsenoside Rb1 (G-Rb1) from Panax ginseng root by intestinal bacterial flora, was explored. Bovine serum albumin (BSA) was coupled to the C-26 position on the
Autor:
Teruaki Akao, Kyoichi Kobashi
Publikováno v:
Bioscience and Microflora. 16:1-7
Autor:
Masao Maruno, Kazuhisa Ishihara, Teruaki Akao, Yoko Wakui, Sakae Amagaya, Shuichi Takeda, Kyoichi Kobashi
Publikováno v:
Journal of Pharmacy and Pharmacology. 48:902-905
To clarify the metabolic fate of glycyrrhizin when orally ingested, we investigated the bioavailability of glycyrrhetic acid, the aglycone of glycyrrhizin, after intravenous or oral administration of glycyrrhetic acid (5.7 mg kg−1, equimolar to gly
Publikováno v:
Biological and Pharmaceutical Bulletin. 19:701-704
Bifidobacterium sp. strain SEN was isolated and characterized by hydrolytic conversion of sennosides to sennidins (Akao et al., Appl. Environ. Microbiol., 60, 1041 (1994)). The sennoside-hydrolyzing capacity of the strain SEN was disappeared followin
Publikováno v:
Biological and Pharmaceutical Bulletin. 19:1121-1125
A beta-glucosidase (EC 3.2.1.21.) was purified 2500-fold from Bacteroides JY-6, an intestinal anaerobic bacterium of human. The specific activity of the homogeneously purified enzyme was 210 mumol/min/mg protein. The enzyme (M(r) 75kDa) was an monome
Publikováno v:
Biological and Pharmaceutical Bulletin. 19:705-709
A novel beta-glucosidase, which is inducible and capable of catalyzing the hydrolysis of sennosides, was purified from Bifidobacterium sp. strain SEN with Triton X-100 solubilization and DEAE-cellulose column chromatography, by which hydrolytic activ