The Experts below are selected from a list of 21378 Experts worldwide ranked by ideXlab platform
A G J Voragen - One of the best experts on this subject based on the ideXlab platform.
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reversed phase and size exclusion chromatography of milk protein hydrolysates relation between elution from reversed phase column and Apparent Molecular Weight distribution
International Dairy Journal, 2001Co-Authors: Cornelly Van Der Ven, Harry Gruppen, Dries B A De Bont, A G J VoragenAbstract:Abstract Hydrolysates of casein and whey protein were analysed with size exclusion and reversed phase chromatography. Hydrolysate elution patterns obtained from the two chromatographic techniques were correlated. The Apparent Molecular Weight distribution (MWD) of the peptide mixtures could be predicted accurately from their reversed phase chromatograms, using partial least squares regression. Reversed phase profiles of specific Molecular Weight fractions overlapped considerably, indicating that the relation between reversed phase chromatography and MWD is complex. Retention times of defined casein peptides on reversed phase column were predicted by summing retention time coefficients of the constituent amino acids. The coefficients were calculated by linear regression from a data set of peptide sequences and retention times obtained from LC/MS analysis of casein hydrolysates. The newly calculated retention time coefficients resulted in better prediction of retention time of casein peptides than did prediction with coefficients from literature.
Nisse Kalkkinen - One of the best experts on this subject based on the ideXlab platform.
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purification and partial sequence analysis of the soluble catechol o methyltransferase from human placenta comparison to the rat liver enzyme
Biochemical and Biophysical Research Communications, 1991Co-Authors: Carola Tilgmann, Nisse KalkkinenAbstract:Catechol-o-methyltransferase from human placenta was purified 1400-fold by hydroxyapatite adsorption, ammonium sulfate precipitation, gel filtration, high performance anion- exchange and reversed-phase chromatography. The purified enzyme has an Apparent Molecular Weight of 26.000, an isoelectric point of 5,3 and is activated ten-fold in the presence of 20mM cysteine. The enzyme shows primary structure homology to the corresponding rat liver soluble enzyme, based on the sequenced tryptic peptides.
Cornelly Van Der Ven - One of the best experts on this subject based on the ideXlab platform.
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reversed phase and size exclusion chromatography of milk protein hydrolysates relation between elution from reversed phase column and Apparent Molecular Weight distribution
International Dairy Journal, 2001Co-Authors: Cornelly Van Der Ven, Harry Gruppen, Dries B A De Bont, A G J VoragenAbstract:Abstract Hydrolysates of casein and whey protein were analysed with size exclusion and reversed phase chromatography. Hydrolysate elution patterns obtained from the two chromatographic techniques were correlated. The Apparent Molecular Weight distribution (MWD) of the peptide mixtures could be predicted accurately from their reversed phase chromatograms, using partial least squares regression. Reversed phase profiles of specific Molecular Weight fractions overlapped considerably, indicating that the relation between reversed phase chromatography and MWD is complex. Retention times of defined casein peptides on reversed phase column were predicted by summing retention time coefficients of the constituent amino acids. The coefficients were calculated by linear regression from a data set of peptide sequences and retention times obtained from LC/MS analysis of casein hydrolysates. The newly calculated retention time coefficients resulted in better prediction of retention time of casein peptides than did prediction with coefficients from literature.
Antonio Marcilla - One of the best experts on this subject based on the ideXlab platform.
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identification of enolase as a plasminogen binding protein in excretory secretory products of fasciola hepatica
FEBS Letters, 2004Co-Authors: Dolores Bernal, Rafael Toledo, José Enrique De La Rubia, Ana M Carrascoabad, Santiago Mascoma, Antonio MarcillaAbstract:We have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host–parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an Apparent Molecular Weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.
Carola Tilgmann - One of the best experts on this subject based on the ideXlab platform.
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purification and partial sequence analysis of the soluble catechol o methyltransferase from human placenta comparison to the rat liver enzyme
Biochemical and Biophysical Research Communications, 1991Co-Authors: Carola Tilgmann, Nisse KalkkinenAbstract:Catechol-o-methyltransferase from human placenta was purified 1400-fold by hydroxyapatite adsorption, ammonium sulfate precipitation, gel filtration, high performance anion- exchange and reversed-phase chromatography. The purified enzyme has an Apparent Molecular Weight of 26.000, an isoelectric point of 5,3 and is activated ten-fold in the presence of 20mM cysteine. The enzyme shows primary structure homology to the corresponding rat liver soluble enzyme, based on the sequenced tryptic peptides.