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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
    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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