title: Purification to single isoforms of a secreted epidermal growth factor receptor in a multicompartment electrolyzer with isoelectric membranes.
abstract: A purified, size-homogeneous (100 kDa), desialylated form of a truncated, soluble form of the epidermal growth factor receptor secreted by A431 human tumor cells has been found, by isoelectric focusing in immobilized pH gradients, to consist of two major isoforms (with pIs of 6.96 and 6.71), one intermediate form (pI 6.45) and a number (> 10) of minor components. The two major components have been purified to charge homogeneity by isoelectric focusing in a multicompartment electrolyzer with buffering isoelectric membranes having the following pI values: 5.90, 6.63, 6.76, 6.92, 7.05 and 7.35. Such single pI species are presently used for attempts at crystal growing.
authors.affiliation: Department of Biomedical Sciences and Technologies, University of Milano, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Wenisch
authors.forename: P G
authors.initials: PG
authors.lastname: Righetti
authors.forename: W
authors.initials: W
authors.lastname: Weber
mesh_terms: D066246:ErbB Receptors / Q000302:isolation & purification*; D005069:Evaluation Studies as Topic; D005782:Gels; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing / Q000295:instrumentation / Q000379:methods*; D007526:Isoelectric Point; D008567:Membranes, Artificial
chemical_list: D005782:Gels; D008567:Membranes, Artificial; D066246:ErbB Receptors