Characterization of pepsin-solubilized type I collagen was examined by
a capillary electrophoresis using a capillary coated with alpha-dodec
yl-omega-hydroxy poly(oxyethylene) to reduce protein adsorption and el
ectroosmic flow. A good peak separation for each polypeptide was achie
ved at pH 5.6-6.5. The peaks were assigned to alpha 1, alpha 2, beta 1
1, beta 12, and gamma by gel chromatography and reversed phase HPLC. I
t is found that each a chain signal split into several peaks, reflecti
ng various residues of teropeptide.