Identification and purification of a soluble species of gp120 released by zymolyase treatment of Pneumocystis carinii.
Purified zymolyase containing beta-glucanase activity releases a soluble species of the gp120 component of the high molecular weight surface antigen complex of rat- and human-derived Pneumocystis carinii. We have purified the soluble gp120 from rat-derived P. carinii by concanavalin A-affinity- and hydrophobic-interaction liquid chromatography. A single band was detected in this fraction by silver staining and immunoblotting. We have also partially purified a soluble form of the corresponding high molecular weight surface antigen from human-derived P. carinii. Identification and purification of a nondenatured soluble species of gp120 will assist in the characterization of its interactions within the surface antigen complex and with host molecules.
Linke
M J
MJ
Department of Internal Medicine, University of Cincinnati College of Medicine, OH 45267-0560.
Walzer
P D
PD
D000818:Animals; D002846:Chromatography, Affinity; D002847:Chromatography, Agarose; D003208:Concanavalin A; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004693:Glucan Endo-1,3-beta-D-Glucosidase; D006023:Glycoproteins / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D011010:Pneumocystis / Q000737:chemistry*; D051381:Rats; D012995:Solubility
D005656:Fungal Proteins; D006023:Glycoproteins; D003208:Concanavalin A; D004693:Glucan Endo-1,3-beta-D-Glucosidase