Institute of Biological Chemistry and Graduate Program in Plant Physiology, Washington State University, Pullman, Washington 99164-6340.
Plant Physiol. 1985 Jun;78(2):241-5. doi: 10.1104/pp.78.2.241.
Wheat coleoptiles have two distinct invertases, a soluble and a cell wall-bound form as indicated by results from cytochemical and biochemical studies. These enzyme activities differ in their pH optima, chromatographic behavior on diethylaminoethyl cellulose, kinetic properties, thermal stability, and response to light treatment. The soluble invertase was purified to near homogeneity by diethylaminoethyl-cellulose, concanavalin-A Sepharose, and Sephacryl S-300 chromatography. The overall purification was 175-fold with a recovery of about 26%. The holoenzyme has an apparent molecular weight of 158,000 and subunit molecular weight of 53,000 as estimated by polyacrylamide gel electrophoresis under denaturing conditions. Illumination of wheat seedlings caused an increase in the cell wall, but not the soluble, invertase activity.
小麦胚芽鞘有两种不同的转化酶，一种是可溶的，一种是细胞壁结合的，这是细胞化学和生化研究的结果。这些酶的活性在 pH 最优值、在二乙基氨基乙基纤维素上的色谱行为、动力学特性、热稳定性以及对光处理的反应方面有所不同。通过 DEAE-纤维素、伴刀豆球蛋白 A-琼脂糖和 Sephacryl S-300 层析，可将可溶性转化酶纯化至近均一状态。总体纯化度为 175 倍，回收率约为 26%。全酶的表观分子量为 158000，亚基分子量为 53000，这是通过在变性条件下进行聚丙烯酰胺凝胶电泳估计的。光照小麦幼苗会导致细胞壁转化酶活性增加，但不影响可溶性转化酶活性。
