Complementation on Ribosomes

作者：David Zipser, Dawn R. Perrin · 发表于：Cold Spring Harbor Symposia on Quantitative Biology · 年份：1963 · DOI：10.1101/sqb.1963.028.01.071 · 被引用次数：51 · 研究领域：RNA and protein synthesis mechanisms、Bacteriophages and microbial interactions、Glycosylation and Glycoproteins Research

Many polypeptide chains do not acquire enzymatic activity until they aggregate into a multimeric protein molecule. In these cases, the "active site" must spread over more than one chain, or, as we now guess more likely, aggregation causes conformational changes leading to enzymatic activity. Among these proteins is the bacterial enzyme β-galactosidase, whose smallest active form sediments at 16S and has a molecular weight generally thought to be about 500,000. Its subunit construction is clearly shown by its disaggregation into 4 subunits by 8 M urea (Zipser, 1963). Each of these urea subunits may have several polypeptide chains.