Hong B S
Toxicon. 1982;20(3):535-45. doi: 10.1016/0041-0101(82)90047-2.
A collagenolytic enzyme, with a molecular weight of 58,000 daltons and isoelectric point of 5.1, was isolated and purified from the venom of the rattlesnake Crotalus atrox by Sephadex G-100 gel filtration followed by chromatography on DEAE-Bio-gel A. The enzyme released alpha-chains from beta-chains of the native collagen and cleaved in the helical region similar to other animal collagenases. The enzyme also hydrolyzed the PZ-peptide, however, it did not hydrolyze synthetic substrates for serine protease (such as TAME or ATEE). The enzyme had no hemorrhagic activity. Immunocross-reactivity suggested that only the venom from Crotalidae contain the enzyme.
从西部菱斑响尾蛇毒液中通过葡聚糖凝胶G - 100凝胶过滤，随后在二乙氨基乙基琼脂糖凝胶A上进行层析，分离并纯化出一种胶原分解酶，其分子量为58,000道尔顿，等电点为5.1。该酶从天然胶原蛋白的β链释放出α链，并在螺旋区域进行切割，这与其他动物胶原酶相似。该酶还能水解PZ - 肽，然而，它不能水解丝氨酸蛋白酶的合成底物（如对甲苯磺酰-L-精氨酸甲酯或苯甲酰-L-精氨酸乙酯）。该酶没有出血活性。免疫交叉反应表明只有蝰蛇科的毒液含有这种酶。
