ABSTRACT
A barley oxalate oxidase was purified to homogeneity and the N-terminal sequences of the protein and of two peptides generated by CNBr cleavage of this protein were determined. Searches for similarities in data bank revealed that the sequences are highly homologous to the amino-acid sequence of a wheat protein, germin, which is synthesized de novo during germination. The similarity of the two proteins was confirmed by showing that anti-oxalate oxidase antibodies strongly recognize germin produced in Escherichia coli. We show that like germin, oxalate oxidase is glycosylated, resistant to SDS denaturation, heat stable, and protease resistant. Moreover, oxalate oxidase activity is strongly induced during germination of barley embryos resulting from an accumulation of the protein. Thus, we conclude that barley oxalate oxidase is a germin-like protein.
