DETERGENT-ACTIVATION OF LATENT COLLAGENASE AND RESOLUTION OF ITS COMPONENT MOLECULES
DETERGENT-ACTIVATION OF LATENT COLLAGENASE AND RESOLUTION OF ITS COMPONENT MOLECULES
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DOI：
10.1016/s0006-291x(82)80120-4
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发表时间：
1982-01-01
影响因子：
3.1
通讯作者：
TAYLOR, RE
中科院分区：
文献类型：
--
作者：
BIRKEDALHANSEN, H;TAYLOR, RE
通过短暂暴露于SDS [十二烷基硫酸钠]激活潜伏性胶原酶，并在该洗涤剂存在下通过丙烯酰胺平板凝胶电泳进行解析。在用Triton X-100去除SDS后，通过重叠技术证明SDS-层析图中的特异性胶原酶活性。梭菌胶原酶（MW = 126，000）和从牛牙龈器官培养物中收获的活性胶原酶（MW = 65，000）以单条带迁移，而人成纤维细胞胶原酶在MW 65，000/55，000和50，000/45，000处分解为2条不同的双条带。与胰蛋白酶预孵育导致潜在酶的激活并伴随着较大的双联体的消失。这些数据表明，两组双波段之间存在一种乘积关系。
Latent collagenase was activated by brief exposure to SDS [sodium dodecyl sulfate] and resolved by acrylamide slab gel electrophoresis in the presence of this detergent. Specific collagenase activity in the SDS-electrophoretogram was demonstrated by an overlay technique after removal of SDS by Triton X-100. Clostridial collagenase (MW = 126,000) and active collagenase harvested from bovine gingival organ culture (MW = 65,000) migrated as single bands whereas human fibroblast collagenase was resolved into 2 distinct double bands at MW 65,000/55,000 and 50,000/45,000. Preincubation with trypsin led to activation of latent enzyme and to concomitant disappearance of the larger doublet. The data suggest a precursor-product relationship between the 2 sets of double bands.