Sakai-Suzuki J, Sakaguchi Y, Hoshino S, Matsumoto J J
Comp Biochem Physiol B. 1983;75(3):409-14. doi: 10.1016/0305-0491(83)90349-8.
When the proteinases of the squid mantle muscle were extracted in the presence of dithiothreitol (DTT), the acid proteinase activity increased, indicating that the squid mantle muscle contains a considerable amount of the acid thiol proteinase. The crude extract hydrolyzed neither alpha-N-benzoyl-D,L-arginine-p-nitroanilide (BAPA) nor azocasein, thus refuting the presence of cathepsins B and L in the mantle muscle. The cathepsin D-like proteinase and the acid thiol proteinase were separated by Sephadex A-50 column chromatography. Each of the above partially purified proteinases was able to degrade carp actomyosin at pH 2.5 and 5.0, respectively.
当在二硫苏糖醇（DTT）存在的情况下提取鱿鱼外套膜肌肉的蛋白酶时，酸性蛋白酶活性增加，这表明鱿鱼外套膜肌肉含有相当数量的酸性巯基蛋白酶。粗提取物既不水解α-N-苯甲酰-D,L-精氨酸对硝基苯胺（BAPA），也不水解偶氮酪蛋白，因此反驳了外套膜肌肉中存在组织蛋白酶B和L的说法。通过葡聚糖凝胶A-50柱色谱法分离出类组织蛋白酶D蛋白酶和酸性巯基蛋白酶。上述每种部分纯化的蛋白酶分别能够在pH 2.5和5.0条件下降解鲤鱼肌动球蛋白。
