Hansma H G
J Protozool. 1975 May;22(2):257-9. doi: 10.1111/j.1550-7408.1975.tb05861.x.
The immobilization antigen (i-antigen) fraction of Paramecium aurelia syngen 4 is shown to contain a protease that is activated by mercaptoethaneol. After the protease has been heat-inactivated, the molecular weight of the i-antigen (similar to 250,000 daltons) cannot be decreased by mercaptoethanol treatment. It is demonstrated that the i-antigen is a single polypeptide chain. Reasons are also given why low molecular weight subunits were previously reported by other authors.
已表明，双小核草履虫同宗配合4号的固定抗原（i -抗原）部分含有一种可被巯基乙醇激活的蛋白酶。蛋白酶经热失活后，巯基乙醇处理无法降低i -抗原的分子量（约250,000道尔顿）。已证明i -抗原是一条单一的多肽链。文中还给出了其他作者先前报道存在低分子量亚基的原因。
