Starch phosphorylase isoenzymes in mesophyll and bundle sheath cells of corn leaves

Christian Mateyka, Claus Schnarrenberger
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引用次数: 8

Abstract

Starch phosphorylase from leaves of the C4-plant corn (Zea mays L.) could be separated into two peaks of activity by chromatography on DEAE-cellulose (or by (NH4)2SO4 gradient solubilization). Subsequent polyacrylamide gel electrophoresis under native conditions revealed a slowly migrating phosphorylase for the peak eluting first from DEAE-cellulose and a major, fast migrating phosphorylase for the peak eluting second. The latter peak contained also two very minor bands which migrated even faster than the other two phosphorylases. When phosphorylases were extracted from mesophyll protoplasts and from bundle sheath strands (isolated by the enzymatic isolation procedure) it was the slowly migrating phosphorylase which was associated with the mesophyll cells and the major, fast migrating phosphorylase which originated from the bundle sheath cells. The findings are discussed in view of similar isoenzymes of phosphorylase reported for chloroplasts and cytosol in leaves of C3-plants.

玉米叶片叶肉和束鞘细胞中的淀粉磷酸化酶同工酶
采用deae -纤维素层析法(或(NH4)2SO4梯度增溶法)可将c4植株玉米叶片淀粉磷酸化酶分为两个活性峰。随后在天然条件下的聚丙烯酰胺凝胶电泳显示,deae -纤维素首先有一个缓慢迁移的磷酸化酶进行峰洗脱,其次是一个主要的快速迁移的磷酸化酶进行峰洗脱。后一个峰还包含两个非常小的条带,其迁移速度比其他两个磷酸化酶更快。从叶肉原生质体和束鞘链中提取的磷酸化酶(通过酶分离程序分离)发现,与叶肉细胞相关的是缓慢迁移的磷酸化酶,而主要的、快速迁移的磷酸化酶来自束鞘细胞。结合c3植物叶片叶绿体和细胞质中磷酸化酶的同工酶的报道,讨论了这一发现。
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