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Noriaki Ishioka - One of the best experts on this subject based on the ideXlab platform.
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Optical resolution of Phenylthiohydantoin-amino acids and identification of Phenylthiohydantoin-d-amino acid residue of [d-Ala2]-methionine enkephalin by capillary electrophoresis
Journal of Chromatography A, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Masaaki Senda, Noriaki IshiokaAbstract:Abstract We propose a system of protein sequence analysis with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE. After fractionation of Phenylthiohydantoin (PTH)-amino acids from the protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, o -trimethyl-β-cyclodextrin (TM-β-CD) and others. In addition, optical resolution of all standard PTH- dl -amino acids including PTH- dl -carboxymethyl-Cys (CM-Cys) and cysteic acid (CYA) except for PTH- dl -Lys was successfully developed. The resolution of PTH- dl -Lys could not be reconfirmed due to low reproducibility and the impurities. As a model peptide, [ d -Ala 2 ]-methionine enkephalin ( l -Tyr– d -Ala–Gly– l -Phe– l -Met), was used and the sequence with dl differentiation was completely determined.
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Identification of Chirality of Phenylthiohydantoin-D-Amino Acid Residue of [D-ala2]-Metthionine Enkephalin by Capillary Electrophoresis: Suppression and Control of Racemization Ratio in the Edman Sequencing Method
Journal of Liquid Chromatography & Related Technologies, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Y. Shisa, Y. Satou, M. Senda, Noriaki IshiokaAbstract:Abstract This paper describes the suppression and control of the racemization ratio (D or L/D+L) of Phenylthiohydantoin (PTH) amino acids in the Edman sequencing method. Most of the racemization occurs in the cyclization/cleavage step. Although optimization of partial racemization using a mixture of TFA and boron trifluoride (BF3)-ethyl ether complex, which is effective in suppressing racemization in the cyclization/cleavage reaction. The partial racemization in PTH derivatization is often useful for DL differentiation, because a minor L- or D-peak produced by racemization can be used as an internal standard in CE. Using the partial racemization method with mixed acids as a cyclization/cleavage reagent, the sequence determination of [D-Ala2]-methionine enkephalin, with DL differentiation, was achieved on a sequencer.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis for protein sequencing
Journal of Chromatography A, 1997Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Noriaki IshiokaAbstract:Abstract An advanced method is described for the complete separation of Phenylthiohydantoin (PTH)- dl -amino acids for protein sequencing. Optical resolution of all standard PTH- dl -amino acids was successfully developed using some chiral selectors, although the resolution of only PTH- dl -His and Lys could not be confirmed, due to low reproducibility and the presence of impurities. In addition, mixed chiral selectors for making a single electrolyte with the ability to optically resolve all standard PTH- dl -amino acids were investigated. Using the only resulting electrolyte, sequence determination of [ d -Ala2]-methionine enkephalin, with dl differentiation, was performed.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis and identification of the Phenylthiohydantoin-D-amino acid residue of [D-Ala2]-methionine enkephalin.
Journal of chromatography. A, 1996Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Noriaki IshiokaAbstract:Abstract This is an initial report to propose a protein sequence analysis system with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE system. After fractionation of Phenylthiohydantoin (PTH)-amino acids using a protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, s-escin and others. As a model peptide, [ d -Ala2]-methionine enkephalin ( l -Tyr- d -Ala-Gly- l -Phe- l -Met), was used and the sequence with dl differentiation was determined, with the exception of the fourth amino acid, l -Phe, using our proposed system.
Yasuyuki Kurosu - One of the best experts on this subject based on the ideXlab platform.
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Optical resolution of Phenylthiohydantoin-amino acids and identification of Phenylthiohydantoin-d-amino acid residue of [d-Ala2]-methionine enkephalin by capillary electrophoresis
Journal of Chromatography A, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Masaaki Senda, Noriaki IshiokaAbstract:Abstract We propose a system of protein sequence analysis with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE. After fractionation of Phenylthiohydantoin (PTH)-amino acids from the protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, o -trimethyl-β-cyclodextrin (TM-β-CD) and others. In addition, optical resolution of all standard PTH- dl -amino acids including PTH- dl -carboxymethyl-Cys (CM-Cys) and cysteic acid (CYA) except for PTH- dl -Lys was successfully developed. The resolution of PTH- dl -Lys could not be reconfirmed due to low reproducibility and the impurities. As a model peptide, [ d -Ala 2 ]-methionine enkephalin ( l -Tyr– d -Ala–Gly– l -Phe– l -Met), was used and the sequence with dl differentiation was completely determined.
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Identification of Chirality of Phenylthiohydantoin-D-Amino Acid Residue of [D-ala2]-Metthionine Enkephalin by Capillary Electrophoresis: Suppression and Control of Racemization Ratio in the Edman Sequencing Method
Journal of Liquid Chromatography & Related Technologies, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Y. Shisa, Y. Satou, M. Senda, Noriaki IshiokaAbstract:Abstract This paper describes the suppression and control of the racemization ratio (D or L/D+L) of Phenylthiohydantoin (PTH) amino acids in the Edman sequencing method. Most of the racemization occurs in the cyclization/cleavage step. Although optimization of partial racemization using a mixture of TFA and boron trifluoride (BF3)-ethyl ether complex, which is effective in suppressing racemization in the cyclization/cleavage reaction. The partial racemization in PTH derivatization is often useful for DL differentiation, because a minor L- or D-peak produced by racemization can be used as an internal standard in CE. Using the partial racemization method with mixed acids as a cyclization/cleavage reagent, the sequence determination of [D-Ala2]-methionine enkephalin, with DL differentiation, was achieved on a sequencer.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis for protein sequencing
Journal of Chromatography A, 1997Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Noriaki IshiokaAbstract:Abstract An advanced method is described for the complete separation of Phenylthiohydantoin (PTH)- dl -amino acids for protein sequencing. Optical resolution of all standard PTH- dl -amino acids was successfully developed using some chiral selectors, although the resolution of only PTH- dl -His and Lys could not be confirmed, due to low reproducibility and the presence of impurities. In addition, mixed chiral selectors for making a single electrolyte with the ability to optically resolve all standard PTH- dl -amino acids were investigated. Using the only resulting electrolyte, sequence determination of [ d -Ala2]-methionine enkephalin, with dl differentiation, was performed.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis and identification of the Phenylthiohydantoin-D-amino acid residue of [D-Ala2]-methionine enkephalin.
Journal of chromatography. A, 1996Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Noriaki IshiokaAbstract:Abstract This is an initial report to propose a protein sequence analysis system with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE system. After fractionation of Phenylthiohydantoin (PTH)-amino acids using a protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, s-escin and others. As a model peptide, [ d -Ala2]-methionine enkephalin ( l -Tyr- d -Ala-Gly- l -Phe- l -Met), was used and the sequence with dl differentiation was determined, with the exception of the fourth amino acid, l -Phe, using our proposed system.
Ruedi Aebersold - One of the best experts on this subject based on the ideXlab platform.
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synthesis of the protein sequencing reagent 4 3 pyridinylmethylaminocarboxypropyl phenyl isothiocyanate and characterization of 4 3 pyridinylmethylaminocarboxypropyl Phenylthiohydantoins
Analytical Biochemistry, 1995Co-Authors: Edward J. Bures, David T Chow, Hamish D Morrison, Heinz Nika, Daniel Heß, Ruedi AebersoldAbstract:Abstract We report the synthesis and structural characterization of the novel Edman-type protein-sequencing reagent 4-(3-pyridinylmethylaminocarboxypropyl) phenyl isothiocyanate. A panel of thiohydantoins prepared from this reagent were found stable during liquid chromatography-electrospray mass spectrometry and were detectable at the low femtomole sensitivity level. Furthermore, the signal detected for these compounds in the mass spectrometer was linear from the low femtomole to the low picomole range. The derivatives showed uv absorbance spectra comparable to their Phenylthiohydantoin counterparts. The extinction coefficient for the 4-(3-pyridinylmethylaminocarboxypropyl) phenyl thiohydantoin tyrosine was determined by adsorptive sequence analysis of a synthetic pentapeptide featuring an N-terminal 125I-labeled tyrosine. The sequence data suggest that the reagent will be useful for extended sequence analysis of proteins and peptides using commercially available gas-liquid-phase sequencers.
Noriko Shindo - One of the best experts on this subject based on the ideXlab platform.
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Optical resolution of Phenylthiohydantoin-amino acids and identification of Phenylthiohydantoin-d-amino acid residue of [d-Ala2]-methionine enkephalin by capillary electrophoresis
Journal of Chromatography A, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Masaaki Senda, Noriaki IshiokaAbstract:Abstract We propose a system of protein sequence analysis with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE. After fractionation of Phenylthiohydantoin (PTH)-amino acids from the protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, o -trimethyl-β-cyclodextrin (TM-β-CD) and others. In addition, optical resolution of all standard PTH- dl -amino acids including PTH- dl -carboxymethyl-Cys (CM-Cys) and cysteic acid (CYA) except for PTH- dl -Lys was successfully developed. The resolution of PTH- dl -Lys could not be reconfirmed due to low reproducibility and the impurities. As a model peptide, [ d -Ala 2 ]-methionine enkephalin ( l -Tyr– d -Ala–Gly– l -Phe– l -Met), was used and the sequence with dl differentiation was completely determined.
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Identification of Chirality of Phenylthiohydantoin-D-Amino Acid Residue of [D-ala2]-Metthionine Enkephalin by Capillary Electrophoresis: Suppression and Control of Racemization Ratio in the Edman Sequencing Method
Journal of Liquid Chromatography & Related Technologies, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Y. Shisa, Y. Satou, M. Senda, Noriaki IshiokaAbstract:Abstract This paper describes the suppression and control of the racemization ratio (D or L/D+L) of Phenylthiohydantoin (PTH) amino acids in the Edman sequencing method. Most of the racemization occurs in the cyclization/cleavage step. Although optimization of partial racemization using a mixture of TFA and boron trifluoride (BF3)-ethyl ether complex, which is effective in suppressing racemization in the cyclization/cleavage reaction. The partial racemization in PTH derivatization is often useful for DL differentiation, because a minor L- or D-peak produced by racemization can be used as an internal standard in CE. Using the partial racemization method with mixed acids as a cyclization/cleavage reagent, the sequence determination of [D-Ala2]-methionine enkephalin, with DL differentiation, was achieved on a sequencer.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis for protein sequencing
Journal of Chromatography A, 1997Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Noriaki IshiokaAbstract:Abstract An advanced method is described for the complete separation of Phenylthiohydantoin (PTH)- dl -amino acids for protein sequencing. Optical resolution of all standard PTH- dl -amino acids was successfully developed using some chiral selectors, although the resolution of only PTH- dl -His and Lys could not be confirmed, due to low reproducibility and the presence of impurities. In addition, mixed chiral selectors for making a single electrolyte with the ability to optically resolve all standard PTH- dl -amino acids were investigated. Using the only resulting electrolyte, sequence determination of [ d -Ala2]-methionine enkephalin, with dl differentiation, was performed.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis and identification of the Phenylthiohydantoin-D-amino acid residue of [D-Ala2]-methionine enkephalin.
Journal of chromatography. A, 1996Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Noriaki IshiokaAbstract:Abstract This is an initial report to propose a protein sequence analysis system with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE system. After fractionation of Phenylthiohydantoin (PTH)-amino acids using a protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, s-escin and others. As a model peptide, [ d -Ala2]-methionine enkephalin ( l -Tyr- d -Ala-Gly- l -Phe- l -Met), was used and the sequence with dl differentiation was determined, with the exception of the fourth amino acid, l -Phe, using our proposed system.
Kimie Murayama - One of the best experts on this subject based on the ideXlab platform.
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Optical resolution of Phenylthiohydantoin-amino acids and identification of Phenylthiohydantoin-d-amino acid residue of [d-Ala2]-methionine enkephalin by capillary electrophoresis
Journal of Chromatography A, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Masaaki Senda, Noriaki IshiokaAbstract:Abstract We propose a system of protein sequence analysis with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE. After fractionation of Phenylthiohydantoin (PTH)-amino acids from the protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, o -trimethyl-β-cyclodextrin (TM-β-CD) and others. In addition, optical resolution of all standard PTH- dl -amino acids including PTH- dl -carboxymethyl-Cys (CM-Cys) and cysteic acid (CYA) except for PTH- dl -Lys was successfully developed. The resolution of PTH- dl -Lys could not be reconfirmed due to low reproducibility and the impurities. As a model peptide, [ d -Ala 2 ]-methionine enkephalin ( l -Tyr– d -Ala–Gly– l -Phe– l -Met), was used and the sequence with dl differentiation was completely determined.
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Identification of Chirality of Phenylthiohydantoin-D-Amino Acid Residue of [D-ala2]-Metthionine Enkephalin by Capillary Electrophoresis: Suppression and Control of Racemization Ratio in the Edman Sequencing Method
Journal of Liquid Chromatography & Related Technologies, 1998Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Y. Shisa, Y. Satou, M. Senda, Noriaki IshiokaAbstract:Abstract This paper describes the suppression and control of the racemization ratio (D or L/D+L) of Phenylthiohydantoin (PTH) amino acids in the Edman sequencing method. Most of the racemization occurs in the cyclization/cleavage step. Although optimization of partial racemization using a mixture of TFA and boron trifluoride (BF3)-ethyl ether complex, which is effective in suppressing racemization in the cyclization/cleavage reaction. The partial racemization in PTH derivatization is often useful for DL differentiation, because a minor L- or D-peak produced by racemization can be used as an internal standard in CE. Using the partial racemization method with mixed acids as a cyclization/cleavage reagent, the sequence determination of [D-Ala2]-methionine enkephalin, with DL differentiation, was achieved on a sequencer.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis for protein sequencing
Journal of Chromatography A, 1997Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Yasuyo Satou, Noriaki IshiokaAbstract:Abstract An advanced method is described for the complete separation of Phenylthiohydantoin (PTH)- dl -amino acids for protein sequencing. Optical resolution of all standard PTH- dl -amino acids was successfully developed using some chiral selectors, although the resolution of only PTH- dl -His and Lys could not be confirmed, due to low reproducibility and the presence of impurities. In addition, mixed chiral selectors for making a single electrolyte with the ability to optically resolve all standard PTH- dl -amino acids were investigated. Using the only resulting electrolyte, sequence determination of [ d -Ala2]-methionine enkephalin, with dl differentiation, was performed.
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Optical resolution of Phenylthiohydantoin-amino acids by capillary electrophoresis and identification of the Phenylthiohydantoin-D-amino acid residue of [D-Ala2]-methionine enkephalin.
Journal of chromatography. A, 1996Co-Authors: Yasuyuki Kurosu, Kimie Murayama, Noriko Shindo, Yoshiko Shisa, Noriaki IshiokaAbstract:Abstract This is an initial report to propose a protein sequence analysis system with dl differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE system. After fractionation of Phenylthiohydantoin (PTH)-amino acids using a protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, s-escin and others. As a model peptide, [ d -Ala2]-methionine enkephalin ( l -Tyr- d -Ala-Gly- l -Phe- l -Met), was used and the sequence with dl differentiation was determined, with the exception of the fourth amino acid, l -Phe, using our proposed system.