Synthesis and release of procollagenase by cultured fibroblasts.
Synthesis and release of procollagenase by cultured fibroblasts.
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培养的成纤维细胞合成和释放原胶原酶。
DOI：
10.1016/s0021-9258(17)33514-7
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发表时间：
1976
期刊：
影响因子：
--
通讯作者：
H. Fullmer
中科院分区：
文献类型：
--
作者：
H. Birkedal‐Hansen;C. Cobb;R. E. Taylor;H. Fullmer
在活跃的胶原蛋白合成期间，从无血清和补充血清的成纤维细胞单层培养物中收获无活性的胶原酶。潜伏的胶原酶不水解胶原，也不结合有效的胶原酶抑制剂α 2-巨球蛋白。用胰蛋白酶活化赋予酶在中性pH下以典型方式水解胶原蛋白并与α 2-巨球蛋白形成抑制复合物的能力。通过校准的凝胶过滤法测定的潜伏酶和活性酶的分子量分别为78，000和60，000。数据表明，胶原酶作为酶原以无活性形式从细胞中释放。
An inactive collagenase was harvested from both serum-free and serum-supplemented fibroblast monolayer cultures in periods of active collagen synthesis. The latent collagenase did not hydrolyze collagen and did not bind the potent collagenase inhibitor alpha2-macroglobulin. Activation with trypsin imparted to the enzyme the ability to hydrolyze collagen at neutral pH in a typical manner and to form an inhibited complex with alpha2-macroglobulin. The molecular weights, determined by calibrated gel filtration, were 78,000 and 60,000 for the latent and active enzymes, respectively. The data indicate that collagenase is released from the cells in inactive form, as a zymogen.