Subunit stoichiometry of human proteasomes.

Enzyme & protein Pub Date : 1993-01-01 DOI:10.1159/000468682
K B Hendil, K G Welinder, D Pedersen, W Uerkvitz, P Kristensen
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引用次数: 12

Abstract

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.

人蛋白酶体的亚基化学计量学。
采用二维聚丙烯酰胺凝胶电泳法分离了人胎盘蛋白酶体亚基。测定了单个斑点蛋白质的氨基酸组成。其中一些斑点具有相同的氨基酸组成,证实它们含有相同亚基的同工异构体。来自HeLa细胞的蛋白酶体,用3h -亮氨酸标记,用抗体沉淀并类似地分离成亚基。测量了每个亚基的放射性。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学。人类蛋白酶体的14个主要亚基中的每一个显然都以相同的数量存在。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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