Choy Y M, Wong Y S, Lau K M, Yung K H
Int J Pept Protein Res. 1979 Jul;14(1):1-4. doi: 10.1111/j.1399-3011.1979.tb01913.x.
Cell wall-bound peroxidase isolated from tobacco leaf mesophyll cell walls was found to consist of two isoenzymes (P1 and P2). Each exists in the form of a single subunit with the same molecular weight (35 000) as determined by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Both isoenzymes exhibited maximum activities at 70 degrees. P1 increased to 265% and P2 to 140% of the activities assayed at 27 degrees; below this temperature the two isoenzymes had the same specific activity. On hydrolysis, P1 showed a carbohydrate content of 26.22% when the monosaccharides were analyzed by gas liquid chromatography; P2 gave 21.45%.
从烟草叶片叶肉细胞壁中分离出的细胞壁结合过氧化物酶由两种同工酶(P1和P2)组成。通过十二烷基硫酸钠(SDS)聚丙烯酰胺凝胶电泳测定,每种同工酶均以单一亚基形式存在,分子量相同(35000)。两种同工酶在70摄氏度时均表现出最大活性。P1的活性增加至27摄氏度时测定活性的265%,P2增加至140%;低于该温度时,两种同工酶具有相同的比活性。水解后,通过气相色谱分析单糖时,P1的碳水化合物含量为26.22%;P2为21.45%。