SPECIFIC DEGRADATION OF COLLAGEN MOLECULE BY TADPOLE COLLAGENOLYTIC ENZYME
SPECIFIC DEGRADATION OF COLLAGEN MOLECULE BY TADPOLE COLLAGENOLYTIC ENZYME
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DOI：
10.1073/pnas.54.4.1197
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发表时间：
1965-01-01
影响因子：
11.1
通讯作者：
NAGAI, Y
中科院分区：
文献类型：
--
作者：
GROSS, J;NAGAI, Y
从蝌蚪组织培养物的培养基中分离的酶在中性pH和生理温度下切割从各种哺乳动物皮肤和蝌蚪鳍中提取的天然胶原蛋白分子。酶的攻击发生在一个点上，将b2 2位点的分子切割成两个片段，一个是从A端起分子长度的四分之三，另一个是从B端起分子长度的四分之一，而不破坏任何片段的螺旋结构。攻击的特异性表现为反应混合物粘度的有限下降、不变的旋光度、在圆盘电泳中出现可直接与原始亚基结合的新的快速移动条带以及每个片段形成片段长间距（SLS）。反应产物的变性温度的降低表明这种酶可能制备用于生理降解的胶原的方式。
An enzyme isolated from the culture medium of tadpole tissue cultures cleaves native collagen molecules extracted from a variety of mammalian skins and tadpole fin at neutral pH and physiologic temperatures. Enzymatic attack occurs at one point, severing the molecule at the b2 2 locus into two fragments, one being three quarters the molecular length from the A end and the other one quarter the length from the B end, without disrupting the helical structure of either fragment. The specificity of the attack was manifested by a limited fall in viscosity of the reaction mixture, unchanged optical rotation, appearance of new faster-moving bands in disk electrophoresis directly referable to the original subunits, and the formation of segment long spacing (SLS) from each of the fragments. Reduction of the denaturation temperature of the reaction products suggests the manner in which this enzyme might prepare collagen for physiologic degradation.