Separation and characterization of the isoenzymes of wall-bound peroxidase from cultured Zinnia cells during tracheary element differentiation
Separation and characterization of the isoenzymes of wall-bound peroxidase from cultured Zinnia cells during tracheary element differentiation
复制标题
气管元件分化过程中培养的百日草细胞壁结合过氧化物酶同工酶的分离和表征
作者：
Yasushi Sato;M. Sugiyama;A. Komamine;H. Fukuda
对百日草细胞壁结合过氧化物酶(EC 1.11.1.7)同工酶(P1-P5)进行了分离和鉴定，以了解这些同工酶与木质素生物合成的关系。百合细胞在Percoll溶液中的离心法分离表明，P1、P2和P5存在于分化后的管状细胞中。这些过氧化物酶同工酶通过几个柱层析步骤进行分离。在Phenyl Superose疏水层析过程中，P5活性被分离为P5A和P5B。最终得到了P1、P3、P5A和P5B的酶纯制剂，并对每种同工酶进行了鉴定。最适pH分别为：P1 5.5~6.0，P3 5.0~7.5，P5A 5.0，P5B 4.0。两种同工酶均能有效地氧化松柏醇，而对香豆醇和芥子醇是所有同工酶的较差底物。P3对Ca~(2+)离子有绝对需求。在此基础上，讨论了过氧化物酶同工酶在导管分子分化过程中对木质素形成的可能作用。
Cell wall-bound peroxidase (EC 1.11.1.7) isoenzymes (P1-P5) from cells of Zinnia elegans L. that were differentiating into tracheary elements were separated and characterized to obtain information about the relationships between these isoenzymes and the biosynthesis of lignin. Fractionation of Zinnia cells by centrifugation in solutions of Percoll revealed that P1, P2, and P5 were present in differentiated tracheary elements. These peroxidase isoenzymes were separated by several column-chromatographic steps. During hydrophobic chromatography on Phenyl Superose, P5 activity was separated into activities P5A and P5B. Enzymatically pure preparations of P1, P3, P5A, and P5B were finally obtained and used for the characterization of each isoenzyme. The optimum pH was 5.5–6.0 for P1, 5.0–7.5 for P3, 5.0 for P5A, and 4.0 for P5B. Each of the isoenzymes oxidized coniferyl alcohol efficiently, whereas p-coumaryl alcohol and sinapyl alcohol were poor substrates for all the isoenzymes. An absolute requirement for Ca2+ ions was demonstrated for P3. Based on these results, possible roles of peroxidase isoenzymes in the formation of lignin during the differentiation of tracheary elements are discussed.
4-香豆酸：诱导分化为气管元件的百日草叶肉细胞中辅酶 A 连接酶和异过氧化物酶的表达。
影响因子：
7.4
作者：
Church,DL;Galston,AW
通讯作者：
Galston,AW