Minkoff L, Abramowitz J, Damadian R
Physiol Chem Phys. 1976;8(2):167-73.
A protein fraction with actin-like characteristics has been isolated from E. coli. The fraction (referred to as A-L fraction) undergoes reversible increases in molecular weight under the same catalytic conditions that polymerize actin, exhibits a distinct peak on SDS electrophoresis at the characteristic molecular weight for actin, depends primarily on potassium for its polymerization, and is not "polymerized" by sodium. A-L fraction in the monomeric form was eluted in the void volume of a Sepharose 6B column, suggesting a large Stoke's radius and a molecular weight in excess of 400,000. The fraction contained 30% RNA by weight that proved refractory to experimental efforts at removal.
已从大肠杆菌中分离出一种具有肌动蛋白样特性的蛋白质组分。该组分（称为A-L组分）在使肌动蛋白聚合的相同催化条件下，分子量会发生可逆增加，在SDS电泳上呈现出肌动蛋白特征分子量处的明显峰值，其聚合主要依赖钾，且不会被钠“聚合”。单体形式的A-L组分在琼脂糖6B柱的空体积中被洗脱，这表明其斯托克斯半径较大且分子量超过400,000。该组分按重量计含有30%的RNA，事实证明难以通过实验方法去除。
