Hendil K B, Welinder K G, Pedersen D, Uerkvitz W, Kristensen P
August Krogh Institute, University of Copenhagen, Denmark.
Enzyme Protein. 1993;47(4-6):232-40. doi: 10.1159/000468682.
Subunits from human placental proteasomes were separated by two-dimensional polyacrylamide gel electrophoresis. The amino acid composition of proteins from individual spots were determined. Some of the spots had identical amino acid compositions, confirming that they contain isoforms of the same subunit. Proteasomes from HeLa cells, labelled with 3H-leucine, were precipitated with an antibody and similarly separated into subunits. The radioactivity in each subunit was measured. The subunit stoichiometry was then calculated from these data and the leucine contents in the subunits. Each of the 14 major subunits of human proteasomes are apparently present in equal amounts.
通过二维聚丙烯酰胺凝胶电泳分离人胎盘蛋白酶体的亚基。测定各个斑点中蛋白质的氨基酸组成。一些斑点具有相同的氨基酸组成，证实它们包含同一亚基的同工型。用³H-亮氨酸标记的HeLa细胞蛋白酶体，用抗体沉淀并同样分离成亚基。测量每个亚基中的放射性。然后根据这些数据和亚基中的亮氨酸含量计算亚基化学计量比。人蛋白酶体的14个主要亚基中的每一个显然都以等量存在。
