采用0．5mol／L醋酸提取，结合NaCl沉淀法从单环刺蜢（Urechis unicinctus）的体壁中提取酸溶性胶原蛋白（ASC），并对其理化性质作初步研究。紫外光谱分析表明ASC的特征吸收波长位于228nm，初步推断所提取的蛋白为典型的胶原蛋白；氨基酸组成分析表明ASC为典型的Ⅰ型胶原蛋白；聚丙烯酰胺凝胶电泳（SDS．PAGE）结果表明ASC有两条不同的α链（α1和α2链）、β链和γ链，其胶原蛋白中含有二硫键；傅里叶红外光谱（FTIR）分析表明其存在三螺旋结构；示差扫描量热仪（DSC）分析表明热变性温度（td）和热收缩温度（ts）分别为33．6℃和67．5℃。%Acid-soluble collagen （ASC） was prepared from the body wall of Urechis unicinctus through exlraction with 0.5 mol/L acetic acid followed by precipitation with 0.9 mol/L NaCI and its physical and chemical properties were primarily studied. Ultraviolet spectral analysis showed that the characteristic absorption wavelength of ASC was 228 nm, suggesting that it is a typical collagen. Amino acid composition analysis indicated that ASC was a typical type I collagen. SDS polyacrylamide gel electrophoresis （SDS- PAGE） suggested that ASC contained two alpha chains （α1 and α2）, one β chain and one γ chain. It also contained disulfide bonds. Fourier-transform infrared （FTIR） spectral analysis revealed the existence of helical arrangements in the collagen. The thermal denaturation temperature （td） and the thermal shrinkable temperature （ts） were 33.6 and 67.5 ℃, respectively.
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