Torres-Ruiz J A, McFadden B A
Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.
Arch Biochem Biophys. 1988 Feb 15;261(1):196-204. doi: 10.1016/0003-9861(88)90118-x.
A 700-kDa protein composed of 12 apparently identical 60-kDa subunits copurifies with the L8S8 form of ribulose bisphosphate carboxylase/oxygenase (RuBisCO) from Chromatium vinosum. Chromatography on DEAE-Sephadex A-50 separates the two proteins in pure form. On the basis of the highly reproducible copurification and reaction of the 700-kDa protein with antibodies to pea RuBisCO large (L)-subunit-binding protein, the protein from C. vinosum is designated as a putative binding protein (PBP) for RuBisCO. Also the N-terminal sequence of PBP is quite similar to that of both alpha and beta subunits of the L-subunit-binding protein. Our present research suggests that PBP may be a RuBisCO small-subunit-binding protein in C. vinosum. Measurements of RuBisCO activity and of species that immunologically cross react with RuBisCO or PBP (by enzyme-linked immunosorbent assay) establish that levels of the two proteins vary together in C. vinosum grown on different carbon sources.
一种由12个明显相同的60 kDa亚基组成的700 kDa蛋白质，与来自嗜硫小红卵菌的二磷酸核酮糖羧化酶/加氧酶（RuBisCO）的L8S8形式共纯化。在DEAE-葡聚糖A-50上进行色谱分离可得到两种纯形式的蛋白质。基于700 kDa蛋白质与豌豆RuBisCO大亚基（L）结合蛋白抗体的高度可重复共纯化和反应，来自嗜硫小红卵菌的该蛋白质被指定为RuBisCO的假定结合蛋白（PBP）。此外，PBP的N端序列与L亚基结合蛋白的α和β亚基的序列非常相似。我们目前的研究表明，PBP可能是嗜硫小红卵菌中的RuBisCO小亚基结合蛋白。通过测量RuBisCO活性以及与RuBisCO或PBP发生免疫交叉反应的物种（通过酶联免疫吸附测定）发现，在以不同碳源生长的嗜硫小红卵菌中，这两种蛋白质的水平会一起变化。
