Hu C F, van Huystee R B
Department of Plant Sciences, University of Western Ontario London, Canada.
Biochem Biophys Res Commun. 1989 Sep 15;163(2):689-94. doi: 10.1016/0006-291x(89)92278-x.
Antibodies against both the native and the deglycosylated cationic peanut peroxidase (C.PRX) were used to probe the structural relationship of this isozyme with its anionic counterpart. Not only the native but also the deglycosylated forms of the cationic and the anionic peroxidases reacted with both antibodies. The activity of the cationic isozymes was inhibited by anti-native C.PRX. Similar but nevertheless distinct immunodetection patterns resulted from reaction of the partially digested cationic and anionic peroxidase peptides with antibodies directed to the deglycosylated as well as to the native C.PRX, suggesting a similarity in their polypeptide structures.
针对天然和去糖基化阳离子花生过氧化物酶（C.PRX）的抗体被用于探究这种同工酶与其阴离子对应物的结构关系。阳离子和阴离子过氧化物酶的天然形式以及去糖基化形式均与这两种抗体发生反应。阳离子同工酶的活性被抗天然C.PRX抑制。部分消化的阳离子和阴离子过氧化物酶肽段与针对去糖基化以及天然C.PRX的抗体反应产生了相似但仍有差异的免疫检测模式，这表明它们的多肽结构具有相似性。
