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  • 1
    Digitale Medien
    Digitale Medien
    Size-exclusion and high-performance liquid chromatography separation of peptides from peptic haemoglobin hydrolysate obtained by ultrafiltration (1988)
    Springer
    Chromatographia 25 (1988), S. 307-312 
    Details
    ISSN: 1612-1112
    Schlagwort(e): Size-exclusion chromatography ; Column liquid chromatography ; Peptides ; Hydrolysates
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Summary Gel filtration (size-exclusion) and high-performance liquid chromatography have been used to separate peptic peptides from haemoglobin hydrolysate. Elution profiles on Sephadex G-25 displayed nine fractions with molecular weights lower than 6500 daltons. Each fraction was analysed for total amino acid content and showed less than 1% free amino acids. Reversed phase HPLC, using ammonium acetate buffer and acetonitrile as solvent, was applied to each fraction in order to obtain pure peptide peaks. The importance of acquiring a better knowledge of such an hydrolysate is discussed. Various potential applications of this type of hydrolysate, some of them already being undertaken, are envisaged.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02324705
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    LC-MS of enzymatic peptic haemoglobin hydrolysate produced at the pilot-plant level (1989)
    Springer
    Chromatographia 27 (1989), S. 128-134 
    Details
    ISSN: 1612-1112
    Schlagwort(e): Column liquid chromatography ; Size-exclusion chromatography ; Fast atom bombardment-MS ; Peptic haemoglobin hydrolysate
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Summary A method is described for the ready identification of any peptide isolated from a complex peptic haemoglobin hydrolysate produced on the pilot-plant scale. A combination of size exclusion and reversed-phase, high-performance liquid chromatography have proved to be a useful strategy for fractionation of such a mixture. This technique enabled pure peptides from the total hydrolysate to be obtained. Amino acid analysis and fast atom bombardment mass spectrometry provided the accurate composition and molecular weight of any isolated peptide. Molecular weights are compared with those deduced from size-exclusion chromatography (SEC) and the usefulness of SEC is discussed. The procedure described in this study will be useful for acquiring a better knowledge of such an hydrolysate and could be extended to other crude protein digests.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02265864
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Semi-preparative purification and characterization of peptides from complex haemoglobin hydrolysate by HPLC-mass spectrometry (1990)
    Springer
    Chromatographia 30 (1990), S. 205-210 
    Details
    ISSN: 1612-1112
    Schlagwort(e): Column liquid chromatography ; Semi-preparative scale purification ; Fast atom bombardment-M S ; Tandem-M S ; Peptic haemoglobin hydrolysate
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Summary An important goal of previous high-performance liquid chromatography (HPLC) studies was the development of a simple procedure for the purification of peptides from very complex haemoglobin enzymatic hydrolysates. This report demonstrates that the separation system described can be used for large sample loadings at laboratory preparative scale (more than 50 mg) without loss of resolution. The efficiency of peptide purification was shown by fast atom bombardment-mass spectrometry (FAB-MS) and tandem mass spectrometry (tandem M S). The procedure described will be of interest in the biotechnology area for the extensive preparation of peptides for fine applications from complex enzymatic hydrolysates.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02274548
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Study of the efficiency of a mobile phase used in size-exclusion HPLC for the separation of peptides from a casein hydrolysate according to their hydrodynamic volume (1991)
    Springer
    Chromatographia 32 (1991), S. 499-504 
    Details
    ISSN: 1612-1112
    Schlagwort(e): Column liquid chromatography ; Size-exclusion ; Peptides ; Casein hydrolysate ; FAB-MS
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Summary A casein hydrolysate was eluted on a TSK G-2000 SW sizeexclusion high-performance liquid chromatography (SE-HPLC) column using a mobile phase which gives a correlation coefficient of 0.98 for the separation of 20 pure and synthetic peptides and proteins of molecular weight (M. W.) varying from 243.28 (Ala-Pro-Gly) to 43 000 (Ovalbumine) daltons. Further isolation and purification of peptides present in each of the 8 different fractions collected from the SE-HPLC were done by reversed-phase HPLC (RP-HPLC). Peptide experimental M. W. determined from the calibration curve obtained for synthetic or purified peptides was compared to their precise M.W. obtained by fast atom bombardment-mass spectrometry analysis (FAB-MS). The results do not show a separation of this complex hydrolysate by SE-HPLC according to the hydrodynamic volume of its constituents.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02327894
    Standort Signatur Erwartet Verfügbarkeit
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