Dumas B, Sailland A, Cheviet J P, Freyssinet G, Pallett K
Laboratoire de Biochimie Moléculaire et Biologie Cellulaire, Rhône-Poulenc Agro, Lyon, France.
C R Acad Sci III. 1993 Aug;316(8):793-8.
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.
一种大麦草酸氧化酶被纯化至同质,并测定了该蛋白质及其经溴化氰裂解产生的两个肽段的N端序列。在数据库中搜索相似性发现,这些序列与一种小麦蛋白(萌发素)的氨基酸序列高度同源,萌发素是在萌发过程中重新合成的。通过证明抗草酸氧化酶抗体能强烈识别大肠杆菌中产生的萌发素,证实了这两种蛋白质的相似性。我们发现,与萌发素一样,草酸氧化酶是糖基化的,对SDS变性有抗性,热稳定且抗蛋白酶。此外,由于蛋白质的积累,大麦胚萌发过程中草酸氧化酶活性被强烈诱导。因此,我们得出结论,大麦草酸氧化酶是一种类萌发素蛋白。