Department of Botany and of Physiology and Cell Biology, University of Kansas, Lawrence, Kansas 66045.
Plant Physiol. 1978 Nov;62(5):794-7. doi: 10.1104/pp.62.5.794.
Preparation and use of a newly developed pH 4.3 horizontal thin layer acrylamide gel which permits the simultaneous separation of acidic and basic isoperoxidases in up to 30 samples is described. Use of cytochrome c, horseradish peroxidase, and a purified potato isoperoxidase as internal standards for a range in isoelectric points of peroxidases from pH 3 to 11 is introduced to facilitate comparison of results obtained with different materials and different methods. Distribution of tissue-specific isoperoxidases in different cell layers of wounded potato (Solanum tuberosum L.) tissue is shown and their purification described. Evidence for the in vitro degradation of basic potato isoperoxidases resulting in more acidic forms similar to isoperoxidases occurring in wounded potato tissue is presented. The significance of this observation for the postulated differential function of different isoperoxidases is discussed.
描述了一种新开发的 pH 4.3 水平薄层层析丙烯酰胺凝胶的制备和使用方法，该凝胶可同时分离多达 30 个样品中的酸性和碱性同工酶。使用细胞色素 c、辣根过氧化物酶和纯化的马铃薯同工酶作为内参，以适应从 pH 3 到 11 的过氧化物同工酶等电点范围，便于比较不同材料和方法获得的结果。展示了不同细胞层的受伤马铃薯（Solanum tuberosum L.）组织中组织特异性同工酶的分布，并描述了它们的纯化过程。提出了同工酶体外降解导致更酸性形式的证据，类似于受伤马铃薯组织中存在的同工酶。讨论了这种观察结果对不同同工酶假设的差异功能的意义。
