遺伝子工学的手法により生産された"生理活性たんぱく質"の結晶化 : インターロイキン-2とインターフェロンを中心として : Part2 生体分子の結晶成長

抄録

Recent developments in gene-engineering and protein purification techniques made it possible to get large amount (say 100 mg) of "physrologrcally active proteins", which play important roles in regulating various biological phenomena, but exist very small amount in natural organisms. These technical trends made feasible various physico-chemical studies of such proteins, including crystallization for X-ray structure analyses. Here, our own experiences on the two types of crystals ofhuman recombinant interleukin-2 (IL-2) are described with special emphases on crystallization conditions, such as supersaturation, pH and nucleation, and crystal growth. Brief descriptions are also given to crystal-lizations of some other proteins, namely interferon-β (IFN-β), tumor necrosis factor (TNF) and epidermal growth factor (EGF).