Demonstration of heterogeneity of chick ovalbumin glycopeptides using 360-MHZ proton magnetic resonance spectroscopy

Abstract

Ovalbumin glycopeptides AC-C and AC-D at various stages of purification were studied by high-field 1H NMR. In a homogeneous substance, the intensity of the various resonances appears in integral amounts, while subintegral intensities usually denote mixtures of structure. Using 1H NMR to nondestructively assay the purification of major components from mixtures is shown. In glycopeptide AC-C there is spectroscopic evidence for the 4 different glycopeptide species, 3 of which have been previously described. A fourth structure not previously reported was detected. In glycopeptide AC-D, there is spectroscopic evidence for 5 different compounds, only 2 of which have been previously reported.