The Experts below are selected from a list of 82194 Experts worldwide ranked by ideXlab platform
Yoshikazu Izumi - One of the best experts on this subject based on the ideXlab platform.
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expression of the vanadium dependent bromoperoxidase gene from a marine macro alga corallina pilulifera in saccharomyces cerevisiae and characterization of the Recombinant Enzyme
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:Abstract The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae . The Enzyme was purified and crystals in “tear drop” form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera . Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 °C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K m values for KBr and H 2 O 2 , and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
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Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the Recombinant Enzyme.
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae. The Enzyme was purified and crystals in "tear drop" form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera. Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 degrees C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K(m) values for KBr and H(2)O(2), and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
Takashi Ohshiro - One of the best experts on this subject based on the ideXlab platform.
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expression of the vanadium dependent bromoperoxidase gene from a marine macro alga corallina pilulifera in saccharomyces cerevisiae and characterization of the Recombinant Enzyme
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:Abstract The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae . The Enzyme was purified and crystals in “tear drop” form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera . Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 °C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K m values for KBr and H 2 O 2 , and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
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Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the Recombinant Enzyme.
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae. The Enzyme was purified and crystals in "tear drop" form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera. Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 degrees C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K(m) values for KBr and H(2)O(2), and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
Wieger Hemrika - One of the best experts on this subject based on the ideXlab platform.
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expression of the vanadium dependent bromoperoxidase gene from a marine macro alga corallina pilulifera in saccharomyces cerevisiae and characterization of the Recombinant Enzyme
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:Abstract The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae . The Enzyme was purified and crystals in “tear drop” form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera . Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 °C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K m values for KBr and H 2 O 2 , and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
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Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the Recombinant Enzyme.
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae. The Enzyme was purified and crystals in "tear drop" form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera. Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 degrees C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K(m) values for KBr and H(2)O(2), and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
Ron Wever - One of the best experts on this subject based on the ideXlab platform.
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expression of the vanadium dependent bromoperoxidase gene from a marine macro alga corallina pilulifera in saccharomyces cerevisiae and characterization of the Recombinant Enzyme
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:Abstract The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae . The Enzyme was purified and crystals in “tear drop” form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera . Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 °C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K m values for KBr and H 2 O 2 , and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
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Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the Recombinant Enzyme.
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae. The Enzyme was purified and crystals in "tear drop" form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera. Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 degrees C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K(m) values for KBr and H(2)O(2), and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
Toshiaki Aibara - One of the best experts on this subject based on the ideXlab platform.
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expression of the vanadium dependent bromoperoxidase gene from a marine macro alga corallina pilulifera in saccharomyces cerevisiae and characterization of the Recombinant Enzyme
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:Abstract The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae . The Enzyme was purified and crystals in “tear drop” form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera . Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 °C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K m values for KBr and H 2 O 2 , and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.
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Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the Recombinant Enzyme.
Phytochemistry, 2002Co-Authors: Takashi Ohshiro, Wieger Hemrika, Toshiaki Aibara, Ron Wever, Yoshikazu IzumiAbstract:The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae. The Enzyme was purified and crystals in "tear drop" form were obtained. The catalytic properties of the Recombinant Enzyme were studied and compared with those of the native Enzyme purified from C. pilulifera. Differences in thermal stability and chloroperoxidase activity were observed. The Recombinant Enzyme retained full activity after preincubation at 65 degrees C for 20 min, but the native Enzyme was completely inactivated under the same conditions. The chlorinating activity of the native Enzyme was more than ten times higher than that of the Recombinant Enzyme. Other properties, such as K(m) values for KBr and H(2)O(2), and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.