Bendikene V G, Vesa V S
Prikl Biokhim Mikrobiol. 1981 May-Jun;17(3):441-7.
Chitin containing sorbents have been obtained for isolation and purification of serine proteases. Serine proteases from Bacillus subtilis have been purified 4-5 times and commercial preparations of trypsin and chymotrypsin 1.5-2 times by chromatography on nondeproteinized chitin. On the benzylated derivative of nondeproteinized chitin complete separation of trypsin and chymotrypsin has been achieved by chromatography of crude pancreatin. It has been shown that the protein moiety of chitin is important for preferential sorption of serine type proteases.
已制备出含几丁质的吸附剂,用于丝氨酸蛋白酶的分离和纯化。通过在非脱蛋白几丁质上进行色谱分离,枯草芽孢杆菌的丝氨酸蛋白酶已被纯化4 - 5倍,胰蛋白酶和胰凝乳蛋白酶的商业制剂已被纯化1.5 - 2倍。在非脱蛋白几丁质的苄基化衍生物上,通过粗制胰酶的色谱分离实现了胰蛋白酶和胰凝乳蛋白酶的完全分离。结果表明,几丁质的蛋白质部分对于丝氨酸型蛋白酶的优先吸附很重要。