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.
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Lemieux, L., Piot, J.M., Guillochon, D. et al. 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. Chromatographia 32, 499–504 (1991). https://doi.org/10.1007/BF02327894
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DOI: https://doi.org/10.1007/BF02327894