Isolation and characterization of one isoform of actin from cultured soybean cells.

Cultured soybean cells (SB-1 cell line) were plasmolyzed and lyophilized. Extraction of the dried powder and fractionation yielded a polypeptide with the following key properties: (a) it has a molecular weight of approximately 45,000 and an isoelectric point of approximately 5.9; (b) it is immunologically cross-reactive with rabbit antibodies affinity purified against the Mr 45,000 polypeptide of calf thymus actin; (c) it is eluted from a DEAE-cellulose column at the same ionic strength as Acanthamoeba actin; (d) it yields peptide maps, after limited proteolysis with V8 protease, similar if not identical to those of rabbit muscle actin; and (e) it binds specifically to deoxyribonuclease I. These molecular and binding properties indicate that we have purified one isoform of actin from soybean cells.