The Experts below are selected from a list of 258 Experts worldwide ranked by ideXlab platform

Hitoshi Sakuraba - One of the best experts on this subject based on the ideXlab platform.

  • only sphingolipid activator protein b sap b or saposin b stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α galactosidase in a detergent free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

  • Only sphingolipid activator protein B (SAP‐B or saposin B) stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α‐galactosidase in a detergent‐free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

Ryoichi Kase - One of the best experts on this subject based on the ideXlab platform.

  • only sphingolipid activator protein b sap b or saposin b stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α galactosidase in a detergent free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

  • Only sphingolipid activator protein B (SAP‐B or saposin B) stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α‐galactosidase in a detergent‐free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

Tse-chao Hua - One of the best experts on this subject based on the ideXlab platform.

  • A thermal biosensor based on Enzyme Reaction.
    Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and, 2005
    Co-Authors: Yi-hua Zheng, Tse-chao Hua
    Abstract:

    Application of the thermal biosensor as analytical tool is promising due to advantages as universal, simplicity and quick response. A novel thermal biosensor based on Enzyme Reaction has been developed. This biosensor is a flow injection analysis system and consists of two channels with Enzyme Reaction column and reference column. The reference column, which is set for eliminating the unspecific heat, is inactived on special Enzyme Reaction of the ingredient to be detected. The special Enzyme Reaction takes places in the Enzyme Reaction column at a constant temperature realizing by a thermoelectric thermostat. Thermal sensor based on the thermoelectric module containing 127 serial BiTe-thermocouples is used to monitor the temperature difference between two streams from the Enzyme Reaction column and the reference column. The analytical example for dichlorvos shows that this biosensor can be used as analytical tool in medicine and biology.

  • A novel thermal biosensor based on Enzyme Reaction for pesticides measurement.
    Journal of environmental sciences (China), 2005
    Co-Authors: Yi-hua Zheng, Tse-chao Hua
    Abstract:

    A novel thermal biosensor based on Enzyme Reaction for pesticides detection has been developed. This biosensor is a flow injection analysis system and consists of two channels with Enzyme Reaction column and identical reference column, which is set for eliminating the unspecific heat. The Enzyme Reaction takes place in the Enzyme Reaction column at a constant temperature (40 degrees C) realized by a thermoelectric thermostat. Thermosensor based on the thermoelectric module containing 127 serial BiTe-thermocouples is used to monitor the temperature difference between two effluents from Enzyme Reaction column and reference column. The ability of this biosensor to detect pesticides is demonstrated by the decreased degree of the hydrolytic heat in two types of thermosensor mode. The hydrolytic Reaction is inhibited by 36% at 1 mg/L DDVP and 50% at 10 mg/L DDVP when cell-typed thermosensor is used. The percent inhibition is 30% at 1 mg/L DDVP and 42% at 10 mg/L DDVP in tube-typed thermosensor mode. The detection for real sample shows that this biosensor can be used for detection of organophosphate pesticides residue.

Minoru Suzuki - One of the best experts on this subject based on the ideXlab platform.

  • only sphingolipid activator protein b sap b or saposin b stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α galactosidase in a detergent free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

  • Only sphingolipid activator protein B (SAP‐B or saposin B) stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α‐galactosidase in a detergent‐free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

Uwe Bierfreund - One of the best experts on this subject based on the ideXlab platform.

  • only sphingolipid activator protein b sap b or saposin b stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α galactosidase in a detergent free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.

  • Only sphingolipid activator protein B (SAP‐B or saposin B) stimulates the degradation of globotriaosylceramide by recombinant human lysosomal α‐galactosidase in a detergent‐free liposomal system
    FEBS Letters, 1996
    Co-Authors: Ryoichi Kase, Uwe Bierfreund, Konrad Sandhoff, Thomas Kolter, Yasuhiro Hashimoto, Kohji Itoh, Andreas Klein, Minoru Suzuki, Hitoshi Sakuraba
    Abstract:

    The degradation of globotriaosylceramide (GbOse3Cer) by insect-cell derived recombinant human α-galactosidase (EC 3.2.1.22) was carried out in a detergent-free liposomal system in order to mimic intralysosomal conditions. GbOse3Cer incorporated into unilamellar liposomes was used as the substrate, and naturally occurring sphingolipid activator proteins, rather than detergents, were used to stimulate the Enzyme Reaction. The degradation of GbOse3Cer was dependent on the presence of both α-galactosidase and sphingolipid activator protein B (SAP-B or saposin B). It proceeded optimally at pH 4.6, and was enhanced by increasing amounts of both α-galactosidase (0.24–24 mU/50 μl assay) and SAP-B (0–5 μg/50 μl assay). The Enzyme Reaction was not affected by SAP-A, SAP-C, or SAP-D. Therefore, our results indicate that only SAP-B is essential for the degradation of GbOse3Cer by α-galactosidase.