蛋白酶 K 对藻胆体中藻胆蛋白之间能量转移的影响。

Effects of proteinase K on the energy transfer between phycobiliproteins in phycobilisomes.

机构信息

Laboratory of Photosynthesis, Institute of Botany, Academia Sinica, Peking, The People's Republic of China.

出版信息

Photosynth Res. 1985 Jan;7(1):91-6. doi: 10.1007/BF00032925.

Abstract

Spectral changes in fluorescence of phycobilisomes (PBS) of A. variabilis treated with proteinase K were studied at room and liquid nitrogen temperature. In control PBS, the relative yield of 77 K fluorescence of F686 was very high, and those of F655 and F666 were low. In PBS treated with proteinase K for less than 1 h, F686 decreased, and F655 and F666 increased. In PBS treated with proteinase K for 2 h, F655 was the main peak of fluorescence emission, F686 was the second peak, the fluorescence emission peak of F666 disappeared. In PBS treated with proteinase K for more than 8 h, F655 showed only one fluorescence emission peak.We suggested that phycobiliporteins in the PBS of A. variabilis constitute an energy transfer chain, shown as follows:{fx91-1}The linkages between APC and APC-B, C-PC and APC, and C-PC and APC-B had different sensitivity towards proteinase K.

摘要

研究了在室温及液氮温度下，用蛋白酶 K 处理变藻蓝蛋白体（PBS）后其荧光的光谱变化。在对照 PBS 中，77 K 荧光的 F686 相对产率很高，而 F655 和 F666 的产率则较低。在经蛋白酶 K 处理不到 1 小时的 PBS 中，F686 减少，F655 和 F666 增加。在经蛋白酶 K 处理 2 小时的 PBS 中，F655 是荧光发射的主要峰，F686 是第二峰，F666 的荧光发射峰消失。在经蛋白酶 K 处理超过 8 小时的 PBS 中，F655 仅显示一个荧光发射峰。我们推测，变藻蓝蛋白体 PBS 中的藻蓝蛋白构成了一个能量传递链，如下所示：{fx91-1}APC 与 APC-B、C-PC 与 APC 和 C-PC 与 APC-B 之间的连接对蛋白酶 K 的敏感性不同。