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Kollipara Padmasree - One of the best experts on this subject based on the ideXlab platform.

  • purification and characterization of a bowman birk proteinase inhibitor from the seeds of black gram vigna mungo
    Phytochemistry, 2010
    Co-Authors: E R Prasad, Aparna Duttagupta, Kollipara Padmasree
    Abstract:

    Abstract A proteinase inhibitor (BgPI) was purified from black gram, Vigna mungo (cv. TAU-1) seeds by using ammonium sulfate fractionation, followed by ion-exchange, affinity and gel-filtration chromatography. BgPI showed a single band in SDS–PAGE under non-reducing condition with an apparent molecular Mass of ∼8 kDa correlating to the peak 8041.5 Da in matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) Mass Spectrum. BgPI existed in different isoinhibitor forms with pI values ranging from 4.3 to 6.0. The internal sequence “SIPPQCHCADIR” of a peak 1453.7 m/z , obtained from MALDI-TOF-TOF showed 100% similarity with Bowman-Birk inhibitor (BBI) family. BgPI exhibited non-competitive-type inhibitory activity against both bovine pancreatic trypsin ( K i of 309.8 nM) and chymotrypsin ( K i of 10.7 μM), however, with a molar ratio of 1:2 with trypsin. BgPI was stable up to a temperature of 80 °C and active over a wide pH range between 2 and 12. The temperature-induced conformational changes in secondary structure are reversed when BgPI was cooled from 90 to 25 °C. Further, upon reduction with dithiothreitol, BgPI lost both its inhibitory activity as well as secondary structural conformation. Lysine residue(s) present in the reactive site of BgPI play an important role in inhibiting the bovine trypsin activity. The present study provides detailed biochemical characteristic features of a BBI type serine proteinase inhibitor isolated from V. mungo .

  • purification and characterization of a bowman birk proteinase inhibitor from the seeds of black gram vigna mungo
    Phytochemistry, 2010
    Co-Authors: E R Prasad, Aparna Duttagupta, Kollipara Padmasree
    Abstract:

    A proteinase inhibitor (BgPI) was purified from black gram, Vigna mungo (cv. TAU-1) seeds by using ammonium sulfate fractionation, followed by ion-exchange, affinity and gel-filtration chromatography. BgPI showed a single band in SDS-PAGE under non-reducing condition with an apparent molecular Mass of approximately 8kDa correlating to the peak 8041.5Da in matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) Mass Spectrum. BgPI existed in different isoinhibitor forms with pI values ranging from 4.3 to 6.0. The internal sequence "SIPPQCHCADIR" of a peak 1453.7 m/z, obtained from MALDI-TOF-TOF showed 100% similarity with Bowman-Birk inhibitor (BBI) family. BgPI exhibited non-competitive-type inhibitory activity against both bovine pancreatic trypsin (K(i) of 309.8nM) and chymotrypsin (K(i) of 10.7muM), however, with a molar ratio of 1:2 with trypsin. BgPI was stable up to a temperature of 80 degrees C and active over a wide pH range between 2 and 12. The temperature-induced conformational changes in secondary structure are reversed when BgPI was cooled from 90 to 25 degrees C. Further, upon reduction with dithiothreitol, BgPI lost both its inhibitory activity as well as secondary structural conformation. Lysine residue(s) present in the reactive site of BgPI play an important role in inhibiting the bovine trypsin activity. The present study provides detailed biochemical characteristic features of a BBI type serine proteinase inhibitor isolated from V. mungo.

E R Prasad - One of the best experts on this subject based on the ideXlab platform.

  • purification and characterization of a bowman birk proteinase inhibitor from the seeds of black gram vigna mungo
    Phytochemistry, 2010
    Co-Authors: E R Prasad, Aparna Duttagupta, Kollipara Padmasree
    Abstract:

    Abstract A proteinase inhibitor (BgPI) was purified from black gram, Vigna mungo (cv. TAU-1) seeds by using ammonium sulfate fractionation, followed by ion-exchange, affinity and gel-filtration chromatography. BgPI showed a single band in SDS–PAGE under non-reducing condition with an apparent molecular Mass of ∼8 kDa correlating to the peak 8041.5 Da in matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) Mass Spectrum. BgPI existed in different isoinhibitor forms with pI values ranging from 4.3 to 6.0. The internal sequence “SIPPQCHCADIR” of a peak 1453.7 m/z , obtained from MALDI-TOF-TOF showed 100% similarity with Bowman-Birk inhibitor (BBI) family. BgPI exhibited non-competitive-type inhibitory activity against both bovine pancreatic trypsin ( K i of 309.8 nM) and chymotrypsin ( K i of 10.7 μM), however, with a molar ratio of 1:2 with trypsin. BgPI was stable up to a temperature of 80 °C and active over a wide pH range between 2 and 12. The temperature-induced conformational changes in secondary structure are reversed when BgPI was cooled from 90 to 25 °C. Further, upon reduction with dithiothreitol, BgPI lost both its inhibitory activity as well as secondary structural conformation. Lysine residue(s) present in the reactive site of BgPI play an important role in inhibiting the bovine trypsin activity. The present study provides detailed biochemical characteristic features of a BBI type serine proteinase inhibitor isolated from V. mungo .

  • purification and characterization of a bowman birk proteinase inhibitor from the seeds of black gram vigna mungo
    Phytochemistry, 2010
    Co-Authors: E R Prasad, Aparna Duttagupta, Kollipara Padmasree
    Abstract:

    A proteinase inhibitor (BgPI) was purified from black gram, Vigna mungo (cv. TAU-1) seeds by using ammonium sulfate fractionation, followed by ion-exchange, affinity and gel-filtration chromatography. BgPI showed a single band in SDS-PAGE under non-reducing condition with an apparent molecular Mass of approximately 8kDa correlating to the peak 8041.5Da in matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) Mass Spectrum. BgPI existed in different isoinhibitor forms with pI values ranging from 4.3 to 6.0. The internal sequence "SIPPQCHCADIR" of a peak 1453.7 m/z, obtained from MALDI-TOF-TOF showed 100% similarity with Bowman-Birk inhibitor (BBI) family. BgPI exhibited non-competitive-type inhibitory activity against both bovine pancreatic trypsin (K(i) of 309.8nM) and chymotrypsin (K(i) of 10.7muM), however, with a molar ratio of 1:2 with trypsin. BgPI was stable up to a temperature of 80 degrees C and active over a wide pH range between 2 and 12. The temperature-induced conformational changes in secondary structure are reversed when BgPI was cooled from 90 to 25 degrees C. Further, upon reduction with dithiothreitol, BgPI lost both its inhibitory activity as well as secondary structural conformation. Lysine residue(s) present in the reactive site of BgPI play an important role in inhibiting the bovine trypsin activity. The present study provides detailed biochemical characteristic features of a BBI type serine proteinase inhibitor isolated from V. mungo.

Aparna Duttagupta - One of the best experts on this subject based on the ideXlab platform.

  • purification and characterization of a bowman birk proteinase inhibitor from the seeds of black gram vigna mungo
    Phytochemistry, 2010
    Co-Authors: E R Prasad, Aparna Duttagupta, Kollipara Padmasree
    Abstract:

    Abstract A proteinase inhibitor (BgPI) was purified from black gram, Vigna mungo (cv. TAU-1) seeds by using ammonium sulfate fractionation, followed by ion-exchange, affinity and gel-filtration chromatography. BgPI showed a single band in SDS–PAGE under non-reducing condition with an apparent molecular Mass of ∼8 kDa correlating to the peak 8041.5 Da in matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) Mass Spectrum. BgPI existed in different isoinhibitor forms with pI values ranging from 4.3 to 6.0. The internal sequence “SIPPQCHCADIR” of a peak 1453.7 m/z , obtained from MALDI-TOF-TOF showed 100% similarity with Bowman-Birk inhibitor (BBI) family. BgPI exhibited non-competitive-type inhibitory activity against both bovine pancreatic trypsin ( K i of 309.8 nM) and chymotrypsin ( K i of 10.7 μM), however, with a molar ratio of 1:2 with trypsin. BgPI was stable up to a temperature of 80 °C and active over a wide pH range between 2 and 12. The temperature-induced conformational changes in secondary structure are reversed when BgPI was cooled from 90 to 25 °C. Further, upon reduction with dithiothreitol, BgPI lost both its inhibitory activity as well as secondary structural conformation. Lysine residue(s) present in the reactive site of BgPI play an important role in inhibiting the bovine trypsin activity. The present study provides detailed biochemical characteristic features of a BBI type serine proteinase inhibitor isolated from V. mungo .

  • purification and characterization of a bowman birk proteinase inhibitor from the seeds of black gram vigna mungo
    Phytochemistry, 2010
    Co-Authors: E R Prasad, Aparna Duttagupta, Kollipara Padmasree
    Abstract:

    A proteinase inhibitor (BgPI) was purified from black gram, Vigna mungo (cv. TAU-1) seeds by using ammonium sulfate fractionation, followed by ion-exchange, affinity and gel-filtration chromatography. BgPI showed a single band in SDS-PAGE under non-reducing condition with an apparent molecular Mass of approximately 8kDa correlating to the peak 8041.5Da in matrix assisted laser desorption ionization time-of-flight (MALDI-TOF) Mass Spectrum. BgPI existed in different isoinhibitor forms with pI values ranging from 4.3 to 6.0. The internal sequence "SIPPQCHCADIR" of a peak 1453.7 m/z, obtained from MALDI-TOF-TOF showed 100% similarity with Bowman-Birk inhibitor (BBI) family. BgPI exhibited non-competitive-type inhibitory activity against both bovine pancreatic trypsin (K(i) of 309.8nM) and chymotrypsin (K(i) of 10.7muM), however, with a molar ratio of 1:2 with trypsin. BgPI was stable up to a temperature of 80 degrees C and active over a wide pH range between 2 and 12. The temperature-induced conformational changes in secondary structure are reversed when BgPI was cooled from 90 to 25 degrees C. Further, upon reduction with dithiothreitol, BgPI lost both its inhibitory activity as well as secondary structural conformation. Lysine residue(s) present in the reactive site of BgPI play an important role in inhibiting the bovine trypsin activity. The present study provides detailed biochemical characteristic features of a BBI type serine proteinase inhibitor isolated from V. mungo.

Hiroaki Sato - One of the best experts on this subject based on the ideXlab platform.

  • first gut instincts are always right the resolution required for a Mass defect analysis of polymer ions can be as low as oligomeric
    Analytical Chemistry, 2018
    Co-Authors: Thierry Fouquet, Takaya Satoh, Hiroaki Sato
    Abstract:

    Its recent adaptation to low-resolution Mass spectra of polymers using fractional base units raises the question of the minimal resolution needed for a Kendrick Mass defect (KMD) analysis. Intuiting an oligomeric resolution since the Mass of a repeat unit is the sole value to be known, it is challenged by the relative failure of the KMD plots computed from an isotopically resolved matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) Mass Spectrum to display clear alignments in the high Mass range. Another procedure based on the remainders of Kendrick Mass (RKMs) overcomes this pitfall with oligomers perfectly aligned in a new RKM plot. Despite a concomitant degradation of the resolving power and accuracy, with the example of MALDI-TOF/TOF Mass spectra of a variety of homo- and copolymer ions, the RKM procedure still allows a rapid enumeration, assignment, and any further manipulation of all the product ion series in visual RKM plots. Successfully extended to the critical case of a MALDI ...

  • First Gut Instincts Are Always Right: The Resolution Required for a Mass Defect Analysis of Polymer Ions Can Be as Low as Oligomeric
    2018
    Co-Authors: Thierry Fouquet, Takaya Satoh, Hiroaki Sato
    Abstract:

    Its recent adaptation to low-resolution Mass spectra of polymers using fractional base units raises the question of the minimal resolution needed for a Kendrick Mass defect (KMD) analysis. Intuiting an oligomeric resolution since the Mass of a repeat unit is the sole value to be known, it is challenged by the relative failure of the KMD plots computed from an isotopically resolved matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) Mass Spectrum to display clear alignments in the high Mass range. Another procedure based on the remainders of Kendrick Mass (RKMs) overcomes this pitfall with oligomers perfectly aligned in a new RKM plot. Despite a concomitant degradation of the resolving power and accuracy, with the example of MALDI-TOF/TOF Mass spectra of a variety of homo- and copolymer ions, the RKM procedure still allows a rapid enumeration, assignment, and any further manipulation of all the product ion series in visual RKM plots. Successfully extended to the critical case of a MALDI Mass Spectrum recorded with a linear TOF analyzer allowing a bare oligomeric resolution, the RKM plot turns the distributions differing by their end-groups or adducted ion into clear horizontal lines. It eventually gives intuition its due by answering the original question: the minimal resolution required for a Mass defect analysis can be as low as oligomeric with the appropriate formulas

Thierry Fouquet - One of the best experts on this subject based on the ideXlab platform.

  • first gut instincts are always right the resolution required for a Mass defect analysis of polymer ions can be as low as oligomeric
    Analytical Chemistry, 2018
    Co-Authors: Thierry Fouquet, Takaya Satoh, Hiroaki Sato
    Abstract:

    Its recent adaptation to low-resolution Mass spectra of polymers using fractional base units raises the question of the minimal resolution needed for a Kendrick Mass defect (KMD) analysis. Intuiting an oligomeric resolution since the Mass of a repeat unit is the sole value to be known, it is challenged by the relative failure of the KMD plots computed from an isotopically resolved matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) Mass Spectrum to display clear alignments in the high Mass range. Another procedure based on the remainders of Kendrick Mass (RKMs) overcomes this pitfall with oligomers perfectly aligned in a new RKM plot. Despite a concomitant degradation of the resolving power and accuracy, with the example of MALDI-TOF/TOF Mass spectra of a variety of homo- and copolymer ions, the RKM procedure still allows a rapid enumeration, assignment, and any further manipulation of all the product ion series in visual RKM plots. Successfully extended to the critical case of a MALDI ...

  • First Gut Instincts Are Always Right: The Resolution Required for a Mass Defect Analysis of Polymer Ions Can Be as Low as Oligomeric
    2018
    Co-Authors: Thierry Fouquet, Takaya Satoh, Hiroaki Sato
    Abstract:

    Its recent adaptation to low-resolution Mass spectra of polymers using fractional base units raises the question of the minimal resolution needed for a Kendrick Mass defect (KMD) analysis. Intuiting an oligomeric resolution since the Mass of a repeat unit is the sole value to be known, it is challenged by the relative failure of the KMD plots computed from an isotopically resolved matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) Mass Spectrum to display clear alignments in the high Mass range. Another procedure based on the remainders of Kendrick Mass (RKMs) overcomes this pitfall with oligomers perfectly aligned in a new RKM plot. Despite a concomitant degradation of the resolving power and accuracy, with the example of MALDI-TOF/TOF Mass spectra of a variety of homo- and copolymer ions, the RKM procedure still allows a rapid enumeration, assignment, and any further manipulation of all the product ion series in visual RKM plots. Successfully extended to the critical case of a MALDI Mass Spectrum recorded with a linear TOF analyzer allowing a bare oligomeric resolution, the RKM plot turns the distributions differing by their end-groups or adducted ion into clear horizontal lines. It eventually gives intuition its due by answering the original question: the minimal resolution required for a Mass defect analysis can be as low as oligomeric with the appropriate formulas