Countercurrent chromatographic analysis of ovalbumin obtained from various sources using the cross-axis coil planet centrifuge.
The present studies have been conducted to investigate the cause of an unusually broad peak of ovalbumin obtained by countercurrent chromatography (CCC) reported earlier [K. Shinomija et al., J. Chromatogr., 644 (1993) 215]. A series of CCC experiments using our prototyte of the cross-axis coil planet centrifuge revealed that commercial ovalbumin products were classified into two groups: group A formed two peaks of ovalbumin at pH 7.0 and 5.8, while group B showed a relatively sharp single peak in a broad range of pH. Electrophoresis indicated that the group A ovalbumin consisted of both natural and denatured products: the natural ovalbumin is a monomer (Mr 45 000) whereas the denatured products form dimers (Mr 90 000). The abnormally broad peak obtained from the group A ovalbumin at pH 9 is apparently caused by the heterogeneity of the sample protein.
Shinomiya
K
K
College of Parmacy, Nihon University, Narashinodai, Funabashi-shi, Chiba, Japan.
Inokuchi
N
N
Gnabre
J N
JN
Muto
M
M
Kabasawa
Y
Y
Fales
H M
HM
Ito
Y
Y
D000818:Animals; D002642:Chick Embryo; D002853:Chromatography, Liquid / Q000379:methods*; D003377:Countercurrent Distribution; D004529:Egg White; D004591:Electrophoresis, Polyacrylamide Gel; D010047:Ovalbumin / Q000737:chemistry*
D010047:Ovalbumin