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  • 1
    Electronic Resource
    Electronic Resource
    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
    Keywords: Column liquid chromatography ; Size-exclusion ; Peptides ; Casein hydrolysate ; FAB-MS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02327894
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  • 2
    Electronic Resource
    Electronic Resource
    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
    Keywords: Size-exclusion chromatography ; Column liquid chromatography ; Peptides ; Hydrolysates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02324705
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  • 3
    Electronic Resource
    Electronic Resource
    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
    Keywords: Column liquid chromatography ; Size-exclusion chromatography ; Fast atom bombardment-MS ; Peptic haemoglobin hydrolysate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02265864
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  • 4
    Electronic Resource
    Electronic Resource
    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
    Keywords: Column liquid chromatography ; Semi-preparative scale purification ; Fast atom bombardment-M S ; Tandem-M S ; Peptic haemoglobin hydrolysate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02274548
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  • 5
    Electronic Resource
    Electronic Resource
    Opioid peptides derived from hemoglobin: Hemorphins (1997)
    New York : Wiley-Blackwell
    Biopolymers 43 (1997), S. 75-98 
    Details
    ISSN: 0006-3525
    Keywords: hemoglobin ; opioid peptides ; HPLC ; macrophages ; pepsin ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Investigation of hemoglobin peptic hydrolysate has revealed the presence of biologically active peptides with affinity for opioid receptors. Two peptides, VV-hemorphin-7 and LVV-hemorphin-7, were resolved by a combination of size exclusion and reversed phase HPLC. A new spectroscopic method based on the second order derivative spectra analysis of aromatic amino acids has been developed. This method allows qualitative and quantitative evaluation of hemorphins generated by peptic hemoglobin hydrolysis. Using this method, a kinetic study of hemorphins appearance has been undertaken. In this paper, we also evidenced the generation of VV-hemorphin-7 from globin by peritoneal macrophages. In regard to this result, the putative physiological role of hemorphins is discussed. © 1997 John Wiley & Sons, Inc. Biopoly 43: 75-98, 1997
    Additional Material: 23 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Separation of hemoglobin and myoglobin from yellowfin tuna red muscle by ultrafiltration: Effect of pH and ionic strength (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 52 (1996), S. 501-506 
    Details
    ISSN: 0006-3592
    Keywords: separation of tuna hemoglobin and myoglobin by ultrafiltration ; Isoelectric pH ; ionic strength ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Efficiency and selectivity of 30 and 150 kd inorganic ultrafiltration membranes (Techsep) toward tuna hemoglobin and myoglobin were studied. The influence of pH and ionic strength was investigated. Mass flow of myoglobin was higher at its isoelectric pH (8.6) and for low ionic strength (1.5 mM). This result was related to the absence of electrostatic repulsion between myoglobin and the surface of the dynamic membrane. The use of high ionic strength 0.15 M NaCl involved an apparent dimerisation of myoglobin and consequently a lower permeation through the membrane due to the molecular weight increase. The permeation and retention of hemoglobin did not agree with the effect of pH observed with myoglobin (best permeation at isoelectric pH) but followed the behavior of myoglobin. This was explained by a myoglobin concentration 10 times higher than hemoglobin concentration. The yield of retention selectivity was investigated. Selectivity of the membrane at pH 8.6 and 1.5 mM was favorable to myoglobin (increase of 40%) whereas a reversed selectivity was observed at pH 7.3, 0.15 M. © 1996 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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