The Experts below are selected from a list of 309 Experts worldwide ranked by ideXlab platform
Koichi Kato - One of the best experts on this subject based on the ideXlab platform.
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Disulfide bond formation in refolding of thermophilic Fungal Protein disulfide isomerase.
Journal of bioscience and bioengineering, 2001Co-Authors: Takushi Harada, Eiji Kurimoto, Kenrou Tokuhiro, Osamu Asami, Tomoya Sakai, Daisuke Nohara, Koichi KatoAbstract:Disulfide bond formation in the refolding of thermophilic Fungal Protein disulfide isomerase (PDI) was investigated. It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the molecular surface causes deformation of the optimum conformation resulting in a decrease in the thermal stability.
Osamu Asami - One of the best experts on this subject based on the ideXlab platform.
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Disulfide bond formation in refolding of thermophilic Fungal Protein disulfide isomerase.
Journal of bioscience and bioengineering, 2001Co-Authors: Takushi Harada, Eiji Kurimoto, Kenrou Tokuhiro, Osamu Asami, Tomoya Sakai, Daisuke Nohara, Koichi KatoAbstract:Disulfide bond formation in the refolding of thermophilic Fungal Protein disulfide isomerase (PDI) was investigated. It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the molecular surface causes deformation of the optimum conformation resulting in a decrease in the thermal stability.
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Thermophilic Fungal Protein disulfide isomerase.
Methods in enzymology, 1998Co-Authors: Tsutomu Kajino, Osamu Asami, Chie Miyazaki, Masana Hirai, Yukio Yamada, Shigezo UdakaAbstract:Publisher Summary For the study the authors have isolated and characterized a thermostable Protein disulfide isomerase (PDI) from a thermophilic fungus, Humicola insolens . The cDNA encoding the Fungal PDI has been cloned and expressed in Bacillus brevis. PDIs from vertebrates and yeast are relatively heat labile. Even in the case of an algal enzyme that is most stable of the known PDIs, the stability against heat is not enough for industrial use of the enzyme. Hence, there is continuing interest in finding new, stable PDIs. Refolding activity using scrambled ribonuclease (RNase) as a substrate is discussed. The Fungal PDI cDNA is expressed in a heterologous Protein production system using B. brevis as a host. In the purification process, anion-exchange chromatography, lectin affinity chromatography, and high-performance liquid chromatography are discussed. The chapter also presents the data for purification of PDI from the fungus, Humicola insolens . To amplify the DNA fragment around the N-terminal consensus region of Fungal PDI, two oligonucleotides corresponding to the amino acid sequence are synthesized and used as primers for a reverse transcriptase-mediated polymerase chain reaction (RT-PCR).
Xiufen Yang - One of the best experts on this subject based on the ideXlab platform.
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A Fungal Protein elicitor PevD1 induces Verticillium wilt resistance in cotton
Plant cell reports, 2013Co-Authors: Dewen Qiu, Hongmei Zeng, Lihua Guo, Jingjing Yuan, Xiufen YangAbstract:Key message We found that the elicitor PevD1 triggered innate immunity in cotton, which plays an important role in future cotton wilt disease control.
Shigezo Udaka - One of the best experts on this subject based on the ideXlab platform.
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Thermophilic Fungal Protein disulfide isomerase.
Methods in enzymology, 1998Co-Authors: Tsutomu Kajino, Osamu Asami, Chie Miyazaki, Masana Hirai, Yukio Yamada, Shigezo UdakaAbstract:Publisher Summary For the study the authors have isolated and characterized a thermostable Protein disulfide isomerase (PDI) from a thermophilic fungus, Humicola insolens . The cDNA encoding the Fungal PDI has been cloned and expressed in Bacillus brevis. PDIs from vertebrates and yeast are relatively heat labile. Even in the case of an algal enzyme that is most stable of the known PDIs, the stability against heat is not enough for industrial use of the enzyme. Hence, there is continuing interest in finding new, stable PDIs. Refolding activity using scrambled ribonuclease (RNase) as a substrate is discussed. The Fungal PDI cDNA is expressed in a heterologous Protein production system using B. brevis as a host. In the purification process, anion-exchange chromatography, lectin affinity chromatography, and high-performance liquid chromatography are discussed. The chapter also presents the data for purification of PDI from the fungus, Humicola insolens . To amplify the DNA fragment around the N-terminal consensus region of Fungal PDI, two oligonucleotides corresponding to the amino acid sequence are synthesized and used as primers for a reverse transcriptase-mediated polymerase chain reaction (RT-PCR).
Takushi Harada - One of the best experts on this subject based on the ideXlab platform.
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Disulfide bond formation in refolding of thermophilic Fungal Protein disulfide isomerase.
Journal of bioscience and bioengineering, 2001Co-Authors: Takushi Harada, Eiji Kurimoto, Kenrou Tokuhiro, Osamu Asami, Tomoya Sakai, Daisuke Nohara, Koichi KatoAbstract:Disulfide bond formation in the refolding of thermophilic Fungal Protein disulfide isomerase (PDI) was investigated. It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the molecular surface causes deformation of the optimum conformation resulting in a decrease in the thermal stability.
