Singh B K, Conn E E
Arch Biochem Biophys. 1986 May 1;246(2):617-21. doi: 10.1016/0003-9861(86)90317-6.
Highly purified fractions of chorismate mutase 1 and 2 from etiolated seedlings of Sorghum bicolor were used as the antigen for antibody production in BALB/c mice. Tests for antigen-antibody complex formation were made by immunodiffusion, immunoprecipitation, and enzyme-linked immunosorbent assay (ELISA). These tests indicated the presence of specific antibodies for each isoenzyme in their antisera. However, in the same tests, no cross-reaction was found between chorismate mutase 1 and 2 and their antisera. This indicates no immunological similarity between the two isoenzymes of chorismate mutase from sorghum.
从高粱黄化幼苗中高度纯化的分支酸变位酶1和2组分被用作抗原,在BALB/c小鼠中产生抗体。通过免疫扩散、免疫沉淀和酶联免疫吸附测定(ELISA)对抗抗原-抗体复合物形成进行检测。这些检测表明其抗血清中存在针对每种同工酶的特异性抗体。然而,在相同检测中,分支酸变位酶1和2与其抗血清之间未发现交叉反应。这表明高粱分支酸变位酶的两种同工酶之间不存在免疫相似性。