Sennosides

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 264 Experts worldwide ranked by ideXlab platform

Tsuneo Namba - One of the best experts on this subject based on the ideXlab platform.

Teruaki Akao - One of the best experts on this subject based on the ideXlab platform.

  • A Sennoside-Hydrolyzing β-Glucosidase from Bifidobacterium Sp. Strain SEN Is Inducible
    Biological & Pharmaceutical Bulletin, 1996
    Co-Authors: Ling Yang, Teruaki Akao, Kyoichi Kobashi, Masao Hattori
    Abstract:

    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 following the addition of glucose to the media in spite of good bacterial growth and potent activity hydrolyzing p-nitrophenyl β-D-glucopyranoside (pNPG). In a fructose-containing medium, no such suppressing effect was shown. Following a 10 h incubation in 50 mM potassium phosphate buffer (pH 7.4), the sennoside-hydrolyzing activity of the bacterium increased, dose-dependently, with the addition of sennoside B. Inhibition of the substrate-induced increase in sennoside-hydrolyzing activity was observed following the addition of some antibiotics (chloramphenicol, streptomycin, and rifampicin). In particular, chloramphenicol completely inhibited the increase of sennoside-hydrolyzing activity while 38% pNPG-hydrolyzing activity remained. It is suggested that the strain SEN produces two different β-glucosidases of which the sennoside-hydrolyzing enzyme is inducible. In addition, the glucosides pNPG, esculin, salicin, or amygdalin stimulated the induction of the sennoside β-glucosidase, but less markedly than sennoside. Sennidin A or sugars (glucose, fructose, cellobiose, or maltose) did not induce the enzyme.

  • isolation of a human intestinal anaerobe bifidobacterium sp strain sen capable of hydrolyzing Sennosides to sennidins
    Applied and Environmental Microbiology, 1994
    Co-Authors: Teruaki Akao, Kyoichi Kobashi, Ling Yang, Masao Hattori, Tsuneo Namba
    Abstract:

    A strictly anaerobic bacterium capable of metabolizing Sennosides was isolated from human feces and identified as Bifidobacterium sp., named strain SEN. The bacterium hydrolyzed Sennosides A and B to sennidins A and B via sennidin A and B 8-monoglucosides, respectively. Among nine species of Bifidobacterium having beta-glucosidase activity, only Bifidobacterium dentium and B. adolescentis metabolized sennoside B to sennidin B, suggesting that the sennoside-metabolizing bacteria produce a novel type of beta-glucosidase capable of hydrolyzing Sennosides to sennidins.

Masao Hattori - One of the best experts on this subject based on the ideXlab platform.

  • A Sennoside-Hydrolyzing β-Glucosidase from Bifidobacterium Sp. Strain SEN Is Inducible
    Biological & Pharmaceutical Bulletin, 1996
    Co-Authors: Ling Yang, Teruaki Akao, Kyoichi Kobashi, Masao Hattori
    Abstract:

    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 following the addition of glucose to the media in spite of good bacterial growth and potent activity hydrolyzing p-nitrophenyl β-D-glucopyranoside (pNPG). In a fructose-containing medium, no such suppressing effect was shown. Following a 10 h incubation in 50 mM potassium phosphate buffer (pH 7.4), the sennoside-hydrolyzing activity of the bacterium increased, dose-dependently, with the addition of sennoside B. Inhibition of the substrate-induced increase in sennoside-hydrolyzing activity was observed following the addition of some antibiotics (chloramphenicol, streptomycin, and rifampicin). In particular, chloramphenicol completely inhibited the increase of sennoside-hydrolyzing activity while 38% pNPG-hydrolyzing activity remained. It is suggested that the strain SEN produces two different β-glucosidases of which the sennoside-hydrolyzing enzyme is inducible. In addition, the glucosides pNPG, esculin, salicin, or amygdalin stimulated the induction of the sennoside β-glucosidase, but less markedly than sennoside. Sennidin A or sugars (glucose, fructose, cellobiose, or maltose) did not induce the enzyme.

  • isolation of a human intestinal anaerobe bifidobacterium sp strain sen capable of hydrolyzing Sennosides to sennidins
    Applied and Environmental Microbiology, 1994
    Co-Authors: Teruaki Akao, Kyoichi Kobashi, Ling Yang, Masao Hattori, Tsuneo Namba
    Abstract:

    A strictly anaerobic bacterium capable of metabolizing Sennosides was isolated from human feces and identified as Bifidobacterium sp., named strain SEN. The bacterium hydrolyzed Sennosides A and B to sennidins A and B via sennidin A and B 8-monoglucosides, respectively. Among nine species of Bifidobacterium having beta-glucosidase activity, only Bifidobacterium dentium and B. adolescentis metabolized sennoside B to sennidin B, suggesting that the sennoside-metabolizing bacteria produce a novel type of beta-glucosidase capable of hydrolyzing Sennosides to sennidins.

Ling Yang - One of the best experts on this subject based on the ideXlab platform.

  • A Sennoside-Hydrolyzing β-Glucosidase from Bifidobacterium Sp. Strain SEN Is Inducible
    Biological & Pharmaceutical Bulletin, 1996
    Co-Authors: Ling Yang, Teruaki Akao, Kyoichi Kobashi, Masao Hattori
    Abstract:

    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 following the addition of glucose to the media in spite of good bacterial growth and potent activity hydrolyzing p-nitrophenyl β-D-glucopyranoside (pNPG). In a fructose-containing medium, no such suppressing effect was shown. Following a 10 h incubation in 50 mM potassium phosphate buffer (pH 7.4), the sennoside-hydrolyzing activity of the bacterium increased, dose-dependently, with the addition of sennoside B. Inhibition of the substrate-induced increase in sennoside-hydrolyzing activity was observed following the addition of some antibiotics (chloramphenicol, streptomycin, and rifampicin). In particular, chloramphenicol completely inhibited the increase of sennoside-hydrolyzing activity while 38% pNPG-hydrolyzing activity remained. It is suggested that the strain SEN produces two different β-glucosidases of which the sennoside-hydrolyzing enzyme is inducible. In addition, the glucosides pNPG, esculin, salicin, or amygdalin stimulated the induction of the sennoside β-glucosidase, but less markedly than sennoside. Sennidin A or sugars (glucose, fructose, cellobiose, or maltose) did not induce the enzyme.

  • isolation of a human intestinal anaerobe bifidobacterium sp strain sen capable of hydrolyzing Sennosides to sennidins
    Applied and Environmental Microbiology, 1994
    Co-Authors: Teruaki Akao, Kyoichi Kobashi, Ling Yang, Masao Hattori, Tsuneo Namba
    Abstract:

    A strictly anaerobic bacterium capable of metabolizing Sennosides was isolated from human feces and identified as Bifidobacterium sp., named strain SEN. The bacterium hydrolyzed Sennosides A and B to sennidins A and B via sennidin A and B 8-monoglucosides, respectively. Among nine species of Bifidobacterium having beta-glucosidase activity, only Bifidobacterium dentium and B. adolescentis metabolized sennoside B to sennidin B, suggesting that the sennoside-metabolizing bacteria produce a novel type of beta-glucosidase capable of hydrolyzing Sennosides to sennidins.

Yukihiro Shoyama - One of the best experts on this subject based on the ideXlab platform.

  • Development of eastern blotting technique for sennoside A and sennoside B using anti-sennoside A and anti-sennoside B monoclonal antibodies.
    Phytochemical Analysis, 2009
    Co-Authors: Osamu Morinaga, Seiichi Sakamoto, Hiroyuki Tanaka, Waraporn Putalun, Sorasak Lhieochaiphant, Yukihiro Shoyama
    Abstract:

    Introduction Rhubarb, senna and sennoside-containing preparations are currently widely employed as purgatives. The major active components of these medications are sennoside A (SA) and sennoside B (SB). Objective To develop an eastern blotting technique for the specific visualisation and easy determination of SA and SB in plant extracts for application in the standardisation and authentication of rhubarb and senna. Methodology SA and SB were separated by TLC, transferred to a PVDF membrane, treated with 1-ethyl-3-(3′-dimethylaminopropyl)-carbodiimide hydrochloride solution and finally treated with bovine serum albumin (BSA). The resulting membrane-bound SA–BSA and SB–BSA conjugates were linked to anti-SA and anti-SB monoclonal antibodies (MAbs) and then to secondary antibodies labelled with peroxidase. SA and SB were detected by visualisation of the peroxidase reaction products. Results The limit of detection of the eastern blotting was 62.5 ng for both Sennosides. The method was applied to the immunohistochemical localisation of SA in fresh rhubarb root. Phloem and radiate wood were found to contain higher concentrations of SA compared with other tissues (pith and bud) in agreement with results obtained by ELISA. The concentrations of SA in the phloem, radiate wood, pith and bud were 64.4, 48.1, 15.0 and 1.8 ng/mg fresh weight, respectively. Conclusion The technique described permitted the visualisation of small molecular weight compounds that had been bound to a membrane, using immunostaining. Owing to the specificity of the MAbs, the eastern blotting may prove to be a useful method for the identification of SA and SB in a background containing large amount of impurities. Copyright © 2009 John Wiley & Sons, Ltd.

  • enzyme linked immunosorbent assay for total Sennosides using anti sennside a and anti sennoside b monoclonal antibodies
    Fitoterapia, 2009
    Co-Authors: Osamu Morinaga, Seiichi Sakamoto, Hiroyuki Tanaka, Yukihiro Shoyama
    Abstract:

    Total Sennosides concentration is a very important factor when rhubarb and senna will be used as crude drugs. However, one-step analytical technique for total Sennosides has not been reported except HPLC. An enzyme-linked immunosorbent assay (ELISA) for total Sennosides concentration by using the combination of anti-sennoside A (SA) and anti-sennoside B (SB) monoclonal antibodies (MAbs) in a single assay has been investigated. Total Sennosides concentration in rhubarb and senna samples determined by newly developed assay system showed good agreement with those analyzed by ELISA using anti-SA MAb and anti-SB MAb, respectively.

  • Sennosides a and b production by hairy roots of senna alata l roxb
    Zeitschrift für Naturforschung C, 2006
    Co-Authors: Waraporn Putalun, Hiroyuki Tanaka, Suwat Pimmeuangkao, Wanchai Deeknamkul, Yukihiro Shoyama
    Abstract:

    : Hairy roots of Senna alata transformed with Agrobacterium rhizogenes, strain ATCC 15834 were induced and grown in half-strength Murashige and Skoog (MS) medium. Effects of sucrose contents and hormones on the growth and Sennosides A, B production were investigated. Hairy roots cultured on hormone-free half-strength MS medium containing 5% sucrose under dark condition mostly stimulated the growth of hairy roots and increased the content of Sennosides A and B yielding (169 +/- 4) and (34 +/- 3) microg g(-1) dry wt, respectively.

  • development of a one step immunochromatographic strip test for the detection of Sennosides a and b
    Phytochemical Analysis, 2004
    Co-Authors: Waraporn Putalun, Osamu Morinaga, Hiroyuki Tanaka, Yukihiro Shoyama
    Abstract:

    An immunochromatographic strip test was developed to detect sennoside A (1) and sennoside B (2) using anti-1 and anti-2 monoclonal antibodies. The qualitative assay was based on a competitive immunoassay in which the detector reagent consisted of colloidal gold particles coated with the respective sennoside antibodies. The capture reagents were 1- and 2-human serum albumin (HSA) conjugates immobilised on a nitrocellulose membrane on the test strip. The sample containing 1 and 2, together with detector reagent, passed over the zone where the capture reagents had been immobilised. The analytes in the sample competed for binding to the limited amount of antibodies in the detector reagent with the immobilised 1- and 2-HSA conjugates on the membrane and hence positive samples showed no colour in the capture spot zone. Detection limits for the strip test were 125 ng/mL for both Sennosides. The assay system is useful as a rapid and simple screening method for the detection of 1 and 2 in plants, drugs and body fluids. Copyright © 2004 John Wiley & Sons, Ltd.

  • Production of monoclonal antibody against a major purgative component, sennoside A, its characterization and ELISA
    Analyst, 2000
    Co-Authors: Osamu Morinaga, Hiroyuki Tanaka, Yukihiro Shoyama
    Abstract:

    For immunization, sennoside A was conjugated with bovine serum albumin. The hapten number in an antigen conjugate was determined to be five by matrix-assisted laser desorption/ionization TOF mass spectrometry. A hybridoma secreting monoclonal antibody against sennoside A was produced by fusing splenocytes immunized with sennoside A–bovine serum albumin and a hypoxantine–aminopterin–thymidine (HAT)-sensitive mouse myeloma cell line, P3-X63-Ag8-653. Weak cross-reactivities occurred with sennoside B which is a stereochemical isomer, and a monomer of sennoside A, rhein, but no cross-reactivities were observed with other related anthraquinones and phenolics. The full range of the assay extends from 20 to 200 ng ml−1 of sennoside A. Good correlation of sennoside A concentrations in crude extract of rhubarb between ELISA and HPLC methods was obtained. The contents of sennoside A in various rhubarb roots were assayed by the newly established ELISA indicating a good agreement with the previous reports.

Related terms

Sennosides - 15 days free trial to Access Experts & Abstracts