Musgrove J E, Johnson R A, Ellis R J
Eur J Biochem. 1987 Mar 16;163(3):529-34. doi: 10.1111/j.1432-1033.1987.tb10900.x.
The ribulosebisphosphate-carboxylase large-subunit binding protein from Pisum sativum chloroplasts is an oligomer of two types of subunit with the composition alpha 6 beta 6. These two subunits are immunologically distinct, show different partial protease digestion patterns and have different amino-terminal sequences. Leaves of Hordeum vulgare also contain an oligomeric binding protein composed of equal amounts of two types of subunit. Treatment of either P. sativum stromal extracts or purified binding protein with ATP and Mg2+ ions causes the dissociation of the oligomeric form of the binding protein to the monomeric subunits. This effect is highly specific for ATP since CTP, UTP, GTP, ADP, AMP, cyclic AMP, NADPH and pyrophosphate do not cause dissociation.
来自豌豆叶绿体的核酮糖二磷酸羧化酶大亚基结合蛋白是由两种亚基组成的寡聚体，其组成为α6β6。这两种亚基在免疫上是不同的，表现出不同的部分蛋白酶消化模式，并且具有不同的氨基末端序列。大麦叶片也含有一种由等量的两种亚基组成的寡聚结合蛋白。用ATP和Mg2+离子处理豌豆基质提取物或纯化的结合蛋白会导致结合蛋白的寡聚形式解离为单体亚基。这种效应对ATP具有高度特异性，因为CTP、UTP、GTP、ADP、AMP、环AMP、NADPH和焦磷酸不会导致解离。
