Comparison of normal down-flow column and new radial-flow column on rapid separation of proteins in egg white

Performance of a new radial-flow column (Sepragen Corporation) was compared with that of a conventional down-flow column on separation of proteins in egg white. Further, a method for analysis of proteins in egg white was developed: Following results were obtained. 1) A rapid analytical method for pr...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nippon Kagakukai shi (1972) 1990, Vol.1990 (1), p.42-47
Hauptverfasser: MORITA, Yazaemon, KAWAKAMI, Minoru, INOUE, Takeshi, KANAI, Satomi
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Performance of a new radial-flow column (Sepragen Corporation) was compared with that of a conventional down-flow column on separation of proteins in egg white. Further, a method for analysis of proteins in egg white was developed: Following results were obtained. 1) A rapid analytical method for proteins in egg white by high performance liq uid chromatography employed aminopropyl bonded silica was established, and the method was successfully applied to identify proteins in fractions separated by preparative scale chromatography. 2) In the case of soft packing material such as DEAE cellulose, the separa ble performance of the radial-flow column with large cross section at flow direction of eluent was superior to that of the conventional down-flow column with small cross section. Proteins in egg white were separated into 3 fractions; ovoglobulins containing lysozyme, ovomucoids containing ovotransferrin, and ovalbumin. 3) In the case of rigid packing material such as hydroxyapatite, the separable performance of the conventional down-flow column was superior to that of the radial-flow column since the down-flow column can withstand high pressure to pack up the packing material. Proteins in egg white were separated into 4 fractions. The fractions were eluted in the order with increasing isoelectric points; ovomucoids (3.9-4.3), ovalbumin (4.5-4.8), ovoglobulins containing ovotransferrin (5.5-6.6), and lysozy me (10-11).
ISSN:0369-4577
2185-0925
DOI:10.1246/nikkashi.1990.42