The Experts below are selected from a list of 49956 Experts worldwide ranked by ideXlab platform

Songping Liang - One of the best experts on this subject based on the ideXlab platform.

  • high throughput analysis of rat Liver plasma Membrane proteome by a nonelectrophoretic in gel tryptic digestion coupled with mass spectrometry identification
    Journal of Proteome Research, 2008
    Co-Authors: Rui Cao, Jian Zhou, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Songping Liang
    Abstract:

    In-gel digestion is commonly used after proteins are resolved by polyacrylamide gel electrophoresis (SDS-PAGE, 2-DE). It can also be used on its own in conjunction with tandem mass spectrometry (MS/MS) for the direct analysis of complex proteins. Here, we describe a strategy combining isolation of purified plasma Membrane, efficient digestion of plasma Membrane proteins in polyacrylamide gel, and high-sensitivity analysis by advanced mass spectrometry to create a new rapid and high-throughput method. The plasma Membrane protein mixture is directly incorporated into a polyacrylamide gel matrix, After formation of the gel, proteins in the gel section are digested with trypsin, and the resulting peptides are subjected to reversed-phase, high-performance liquid chromatography followed by electrospray ion-trap tandem mass analysis. Using this optimized strategy, we have identified 883 rat Liver Membrane proteins, of which 490 had a gene ontology (GO) annotation indicating a cellular component, and 294 (60%) of the latter were known integral Membrane proteins or Membrane proteins. In total, 333 proteins are predicted by the TMHMM 2.0 algorithm to have transMembrane domains (TMDs) and 52% (175 of 333) proteins to contain 2-16 TMDs. The identified Membrane proteins provide a broad representation of the rat plasma Membrane proteome with little bias evident due to protein p I and molecular weight (MW). Also, Membrane proteins with a high GRAVY score (grand average hydrophobicity score) were identified, and basic and acidic Membrane proteins were evenly represented. This study not only offered an efficient and powerful method in shotgun proteomics for the identification of proteins of complex plasma Membrane samples but also allowed in-depth study of Liver Membrane proteomes, such as of rat models of Liver-related disease. This work represents one of the most comprehensive proteomic analyses of the Membrane subproteome of rat Liver plasma Membrane in general.

  • integration of a two phase partition method into proteomics research on rat Liver plasma Membrane proteins
    Journal of Proteome Research, 2006
    Co-Authors: Rui Cao, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Xia Peng, Songping Liang
    Abstract:

    To comprehensively identify proteins of the rat Liver plasma Membrane (PM), we have adopted a proteomics strategy that utilizes sucrose density centrifugation in conjunction with aqueous two-phase partition for plasma Membrane isolation, followed by SDS-PAGE, mass spectrometry and bioinformatics. Western blot analysis showed that this method results in highly purified plasma Membrane fractions, which is a key to successful plasma Membrane proteomics. The PM proteins were separated by SDS-PAGE and digested with trypsin. Through nano-ESI-LC MS/MS analysis we identified 428 rat Liver Membrane proteins, of which 304 had a gene ontology (GO) annotation indicating a cellular component, and 204 (67%) of the latter were known integral Membrane proteins or Membrane-associated proteins. In addition to proteins known to be associated with the plasma Membrane, several hypothetical proteins have also been identified. This study not only provides a tool to study plasma Membrane proteins with low levels of contamination, but also provides a data set for proteins of high to moderate abundance in rat Liver plasma Membranes, thus allowing for more comprehensive characterization of Membrane proteins and a better understanding of Membrane dynamics.

Rui Cao - One of the best experts on this subject based on the ideXlab platform.

  • high throughput analysis of rat Liver plasma Membrane proteome by a nonelectrophoretic in gel tryptic digestion coupled with mass spectrometry identification
    Journal of Proteome Research, 2008
    Co-Authors: Rui Cao, Jian Zhou, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Songping Liang
    Abstract:

    In-gel digestion is commonly used after proteins are resolved by polyacrylamide gel electrophoresis (SDS-PAGE, 2-DE). It can also be used on its own in conjunction with tandem mass spectrometry (MS/MS) for the direct analysis of complex proteins. Here, we describe a strategy combining isolation of purified plasma Membrane, efficient digestion of plasma Membrane proteins in polyacrylamide gel, and high-sensitivity analysis by advanced mass spectrometry to create a new rapid and high-throughput method. The plasma Membrane protein mixture is directly incorporated into a polyacrylamide gel matrix, After formation of the gel, proteins in the gel section are digested with trypsin, and the resulting peptides are subjected to reversed-phase, high-performance liquid chromatography followed by electrospray ion-trap tandem mass analysis. Using this optimized strategy, we have identified 883 rat Liver Membrane proteins, of which 490 had a gene ontology (GO) annotation indicating a cellular component, and 294 (60%) of the latter were known integral Membrane proteins or Membrane proteins. In total, 333 proteins are predicted by the TMHMM 2.0 algorithm to have transMembrane domains (TMDs) and 52% (175 of 333) proteins to contain 2-16 TMDs. The identified Membrane proteins provide a broad representation of the rat plasma Membrane proteome with little bias evident due to protein p I and molecular weight (MW). Also, Membrane proteins with a high GRAVY score (grand average hydrophobicity score) were identified, and basic and acidic Membrane proteins were evenly represented. This study not only offered an efficient and powerful method in shotgun proteomics for the identification of proteins of complex plasma Membrane samples but also allowed in-depth study of Liver Membrane proteomes, such as of rat models of Liver-related disease. This work represents one of the most comprehensive proteomic analyses of the Membrane subproteome of rat Liver plasma Membrane in general.

  • integration of a two phase partition method into proteomics research on rat Liver plasma Membrane proteins
    Journal of Proteome Research, 2006
    Co-Authors: Rui Cao, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Xia Peng, Songping Liang
    Abstract:

    To comprehensively identify proteins of the rat Liver plasma Membrane (PM), we have adopted a proteomics strategy that utilizes sucrose density centrifugation in conjunction with aqueous two-phase partition for plasma Membrane isolation, followed by SDS-PAGE, mass spectrometry and bioinformatics. Western blot analysis showed that this method results in highly purified plasma Membrane fractions, which is a key to successful plasma Membrane proteomics. The PM proteins were separated by SDS-PAGE and digested with trypsin. Through nano-ESI-LC MS/MS analysis we identified 428 rat Liver Membrane proteins, of which 304 had a gene ontology (GO) annotation indicating a cellular component, and 204 (67%) of the latter were known integral Membrane proteins or Membrane-associated proteins. In addition to proteins known to be associated with the plasma Membrane, several hypothetical proteins have also been identified. This study not only provides a tool to study plasma Membrane proteins with low levels of contamination, but also provides a data set for proteins of high to moderate abundance in rat Liver plasma Membranes, thus allowing for more comprehensive characterization of Membrane proteins and a better understanding of Membrane dynamics.

Zhen Liu - One of the best experts on this subject based on the ideXlab platform.

  • high throughput analysis of rat Liver plasma Membrane proteome by a nonelectrophoretic in gel tryptic digestion coupled with mass spectrometry identification
    Journal of Proteome Research, 2008
    Co-Authors: Rui Cao, Jian Zhou, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Songping Liang
    Abstract:

    In-gel digestion is commonly used after proteins are resolved by polyacrylamide gel electrophoresis (SDS-PAGE, 2-DE). It can also be used on its own in conjunction with tandem mass spectrometry (MS/MS) for the direct analysis of complex proteins. Here, we describe a strategy combining isolation of purified plasma Membrane, efficient digestion of plasma Membrane proteins in polyacrylamide gel, and high-sensitivity analysis by advanced mass spectrometry to create a new rapid and high-throughput method. The plasma Membrane protein mixture is directly incorporated into a polyacrylamide gel matrix, After formation of the gel, proteins in the gel section are digested with trypsin, and the resulting peptides are subjected to reversed-phase, high-performance liquid chromatography followed by electrospray ion-trap tandem mass analysis. Using this optimized strategy, we have identified 883 rat Liver Membrane proteins, of which 490 had a gene ontology (GO) annotation indicating a cellular component, and 294 (60%) of the latter were known integral Membrane proteins or Membrane proteins. In total, 333 proteins are predicted by the TMHMM 2.0 algorithm to have transMembrane domains (TMDs) and 52% (175 of 333) proteins to contain 2-16 TMDs. The identified Membrane proteins provide a broad representation of the rat plasma Membrane proteome with little bias evident due to protein p I and molecular weight (MW). Also, Membrane proteins with a high GRAVY score (grand average hydrophobicity score) were identified, and basic and acidic Membrane proteins were evenly represented. This study not only offered an efficient and powerful method in shotgun proteomics for the identification of proteins of complex plasma Membrane samples but also allowed in-depth study of Liver Membrane proteomes, such as of rat models of Liver-related disease. This work represents one of the most comprehensive proteomic analyses of the Membrane subproteome of rat Liver plasma Membrane in general.

  • integration of a two phase partition method into proteomics research on rat Liver plasma Membrane proteins
    Journal of Proteome Research, 2006
    Co-Authors: Rui Cao, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Xia Peng, Songping Liang
    Abstract:

    To comprehensively identify proteins of the rat Liver plasma Membrane (PM), we have adopted a proteomics strategy that utilizes sucrose density centrifugation in conjunction with aqueous two-phase partition for plasma Membrane isolation, followed by SDS-PAGE, mass spectrometry and bioinformatics. Western blot analysis showed that this method results in highly purified plasma Membrane fractions, which is a key to successful plasma Membrane proteomics. The PM proteins were separated by SDS-PAGE and digested with trypsin. Through nano-ESI-LC MS/MS analysis we identified 428 rat Liver Membrane proteins, of which 304 had a gene ontology (GO) annotation indicating a cellular component, and 204 (67%) of the latter were known integral Membrane proteins or Membrane-associated proteins. In addition to proteins known to be associated with the plasma Membrane, several hypothetical proteins have also been identified. This study not only provides a tool to study plasma Membrane proteins with low levels of contamination, but also provides a data set for proteins of high to moderate abundance in rat Liver plasma Membranes, thus allowing for more comprehensive characterization of Membrane proteins and a better understanding of Membrane dynamics.

Xianchun Wang - One of the best experts on this subject based on the ideXlab platform.

  • high throughput analysis of rat Liver plasma Membrane proteome by a nonelectrophoretic in gel tryptic digestion coupled with mass spectrometry identification
    Journal of Proteome Research, 2008
    Co-Authors: Rui Cao, Jian Zhou, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Songping Liang
    Abstract:

    In-gel digestion is commonly used after proteins are resolved by polyacrylamide gel electrophoresis (SDS-PAGE, 2-DE). It can also be used on its own in conjunction with tandem mass spectrometry (MS/MS) for the direct analysis of complex proteins. Here, we describe a strategy combining isolation of purified plasma Membrane, efficient digestion of plasma Membrane proteins in polyacrylamide gel, and high-sensitivity analysis by advanced mass spectrometry to create a new rapid and high-throughput method. The plasma Membrane protein mixture is directly incorporated into a polyacrylamide gel matrix, After formation of the gel, proteins in the gel section are digested with trypsin, and the resulting peptides are subjected to reversed-phase, high-performance liquid chromatography followed by electrospray ion-trap tandem mass analysis. Using this optimized strategy, we have identified 883 rat Liver Membrane proteins, of which 490 had a gene ontology (GO) annotation indicating a cellular component, and 294 (60%) of the latter were known integral Membrane proteins or Membrane proteins. In total, 333 proteins are predicted by the TMHMM 2.0 algorithm to have transMembrane domains (TMDs) and 52% (175 of 333) proteins to contain 2-16 TMDs. The identified Membrane proteins provide a broad representation of the rat plasma Membrane proteome with little bias evident due to protein p I and molecular weight (MW). Also, Membrane proteins with a high GRAVY score (grand average hydrophobicity score) were identified, and basic and acidic Membrane proteins were evenly represented. This study not only offered an efficient and powerful method in shotgun proteomics for the identification of proteins of complex plasma Membrane samples but also allowed in-depth study of Liver Membrane proteomes, such as of rat models of Liver-related disease. This work represents one of the most comprehensive proteomic analyses of the Membrane subproteome of rat Liver plasma Membrane in general.

  • integration of a two phase partition method into proteomics research on rat Liver plasma Membrane proteins
    Journal of Proteome Research, 2006
    Co-Authors: Rui Cao, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Xia Peng, Songping Liang
    Abstract:

    To comprehensively identify proteins of the rat Liver plasma Membrane (PM), we have adopted a proteomics strategy that utilizes sucrose density centrifugation in conjunction with aqueous two-phase partition for plasma Membrane isolation, followed by SDS-PAGE, mass spectrometry and bioinformatics. Western blot analysis showed that this method results in highly purified plasma Membrane fractions, which is a key to successful plasma Membrane proteomics. The PM proteins were separated by SDS-PAGE and digested with trypsin. Through nano-ESI-LC MS/MS analysis we identified 428 rat Liver Membrane proteins, of which 304 had a gene ontology (GO) annotation indicating a cellular component, and 204 (67%) of the latter were known integral Membrane proteins or Membrane-associated proteins. In addition to proteins known to be associated with the plasma Membrane, several hypothetical proteins have also been identified. This study not only provides a tool to study plasma Membrane proteins with low levels of contamination, but also provides a data set for proteins of high to moderate abundance in rat Liver plasma Membranes, thus allowing for more comprehensive characterization of Membrane proteins and a better understanding of Membrane dynamics.

Jingyun Xie - One of the best experts on this subject based on the ideXlab platform.

  • high throughput analysis of rat Liver plasma Membrane proteome by a nonelectrophoretic in gel tryptic digestion coupled with mass spectrometry identification
    Journal of Proteome Research, 2008
    Co-Authors: Rui Cao, Jian Zhou, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Songping Liang
    Abstract:

    In-gel digestion is commonly used after proteins are resolved by polyacrylamide gel electrophoresis (SDS-PAGE, 2-DE). It can also be used on its own in conjunction with tandem mass spectrometry (MS/MS) for the direct analysis of complex proteins. Here, we describe a strategy combining isolation of purified plasma Membrane, efficient digestion of plasma Membrane proteins in polyacrylamide gel, and high-sensitivity analysis by advanced mass spectrometry to create a new rapid and high-throughput method. The plasma Membrane protein mixture is directly incorporated into a polyacrylamide gel matrix, After formation of the gel, proteins in the gel section are digested with trypsin, and the resulting peptides are subjected to reversed-phase, high-performance liquid chromatography followed by electrospray ion-trap tandem mass analysis. Using this optimized strategy, we have identified 883 rat Liver Membrane proteins, of which 490 had a gene ontology (GO) annotation indicating a cellular component, and 294 (60%) of the latter were known integral Membrane proteins or Membrane proteins. In total, 333 proteins are predicted by the TMHMM 2.0 algorithm to have transMembrane domains (TMDs) and 52% (175 of 333) proteins to contain 2-16 TMDs. The identified Membrane proteins provide a broad representation of the rat plasma Membrane proteome with little bias evident due to protein p I and molecular weight (MW). Also, Membrane proteins with a high GRAVY score (grand average hydrophobicity score) were identified, and basic and acidic Membrane proteins were evenly represented. This study not only offered an efficient and powerful method in shotgun proteomics for the identification of proteins of complex plasma Membrane samples but also allowed in-depth study of Liver Membrane proteomes, such as of rat models of Liver-related disease. This work represents one of the most comprehensive proteomic analyses of the Membrane subproteome of rat Liver plasma Membrane in general.

  • integration of a two phase partition method into proteomics research on rat Liver plasma Membrane proteins
    Journal of Proteome Research, 2006
    Co-Authors: Rui Cao, Zhen Liu, Xianchun Wang, Ping Chen, Jingyun Xie, Xia Peng, Songping Liang
    Abstract:

    To comprehensively identify proteins of the rat Liver plasma Membrane (PM), we have adopted a proteomics strategy that utilizes sucrose density centrifugation in conjunction with aqueous two-phase partition for plasma Membrane isolation, followed by SDS-PAGE, mass spectrometry and bioinformatics. Western blot analysis showed that this method results in highly purified plasma Membrane fractions, which is a key to successful plasma Membrane proteomics. The PM proteins were separated by SDS-PAGE and digested with trypsin. Through nano-ESI-LC MS/MS analysis we identified 428 rat Liver Membrane proteins, of which 304 had a gene ontology (GO) annotation indicating a cellular component, and 204 (67%) of the latter were known integral Membrane proteins or Membrane-associated proteins. In addition to proteins known to be associated with the plasma Membrane, several hypothetical proteins have also been identified. This study not only provides a tool to study plasma Membrane proteins with low levels of contamination, but also provides a data set for proteins of high to moderate abundance in rat Liver plasma Membranes, thus allowing for more comprehensive characterization of Membrane proteins and a better understanding of Membrane dynamics.