Partial Purification and Properties of Lupus Erythematosus Cell Promoting Factor

Summary Partial purification of the L-E cell promoting factor from gamma globulin has been achieved with the aid of a cationic cellulose exchanger. The fraction containing L-E activity is eluted at a pH of approximately 7 and a salt concentration of 0.15M. In the process of purification, total prote...

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Veröffentlicht in:Experimental biology and medicine (Maywood, N.J.) N.J.), 1958-12, Vol.99 (3), p.645-648
Hauptverfasser: Willkens, Robert F., Dreschler, Marilyn, Larson, Daniel L.
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Sprache:eng
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Zusammenfassung:Summary Partial purification of the L-E cell promoting factor from gamma globulin has been achieved with the aid of a cationic cellulose exchanger. The fraction containing L-E activity is eluted at a pH of approximately 7 and a salt concentration of 0.15M. In the process of purification, total protein nitrogen content was reduced 97% nitrogen to phosphorus ratio was reduced from 44 to 14.3 without notable reduction in biologic activity. This fraction possesses the electrophoretic, sedimentation and immunologic properties of a normal gamma globulin.
ISSN:0037-9727
1535-3702
1535-3699
DOI:10.3181/00379727-99-24448