Separation of enantiomers on a chiral stationary phase based on ovoglycoprotein. VII. Comparison of chiral recognition ability of ovoglycoprotein from chicken and Japanese quail egg whites.

Ovoglycoproteins from chicken and Japanese quail egg whites (OGCHI and OGJPQ, respectively) were isolated, and characterized by isoelectric focusing, high-performance capillary electrophoresis, reversed-phase HPLC and matrix-assisted laser-desorption ionization time-of-flight (MALDI-TOF) MS. The isoelectric point (pI) of natural OGCHI was 4.37-4.51 by isoelectric focusing, while natural OGJPQ showed two discrete bands at pI 4.68 and 4.77. The average molecular masses of natural OGCHI and OGJPQ were estimated to be about 30000 and 27400 by MALDI-TOF-MS. Both natural OGCHI and OGJPQ were either fully or partially glycosylated with a ratio of ca. 3:1. Next, natural OGCHI and OGJPQ were bound to aminopropyl-silica gels activated with N,N'-disuccinimidylcarbonate to compare retentive and enantioselective properties of the two columns. The OGCHI column is suitable for chiral resolution of basic compounds, while the OGJPQ column is suitable for that of acidic compounds. With regard to chiral resolution of neutral compounds, it is dependent on a compound resolved which column could be suitable. Differences in the retentivity and enantioselectivity between OGCHI and OGJPQ columns are due to differences in the enantioselective binding properties. The results obtained reveal that chiral recognition of various solutes could be efficiently attained by using both columns complementarily.