Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria, 3052 Australia.
Plant Physiol. 1978 May;61(5):768-71. doi: 10.1104/pp.61.5.768.
Chloroplasts isolated from the siphonous green alga Caulerpa simpliciuscula (Turner) C.Ag. were shown to be resistant to dissolution by the nonionic detergent Teric-10 at concentrations as high as 0.3% (v/v) when treated at 0 C. There was little release of stromal enzymes under these conditions. These chloroplasts were disrupted by osmotic shock as shown by measurement of the release of both glucose-6-phosphate dehydrogenase and NADP-dependent glutamate dehydrogenase into the suspending medium. Ribulose-1,5-bisphosphate carboxylase, an accepted marker for chloroplast stromal protein in higher plants, was largely retained in the disrupted chloroplast following the osmotic shock. This is considered to be due to the location of a significant proportion of enzyme within the pyrenoid, which protects it from dissolution and causes it to behave as though it were an insoluble protein.
从管藻科的石莼（Caulerpa simpliciuscula (Turner) C.Ag.）中分离出的叶绿体在 0°C 下用高达 0.3%（v/v）的非离子型去污剂 Teric-10 处理时，即使在高浓度下也能抵抗溶解。在这些条件下，基质酶的释放很少。如通过测量葡萄糖-6-磷酸脱氢酶和 NADP 依赖性谷氨酸脱氢酶释放到悬浮介质中所示，这些叶绿体通过渗透冲击而被破坏。在渗透冲击后，1,5-二磷酸核酮糖羧化酶（Rubisco），一种高等植物叶绿体基质蛋白的公认标志物，大部分保留在被破坏的叶绿体中。这被认为是由于相当一部分酶位于淀粉粒体内，这使其免受溶解并使其表现得好像是不溶性蛋白质。
