Human leukocyte collagenase: characterization of enzyme kinetics by a new method.
Human leukocyte collagenase: characterization of enzyme kinetics by a new method.
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人白细胞胶原酶：通过新方法表征酶动力学。
DOI：
10.1016/0003-2697(77)90059-8
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发表时间：
1977
影响因子：
2.9
通讯作者：
Jouni Uitto
中科院分区：
文献类型：
--
作者：
H. Turto;S. Lindy;V. Uitto;Otto Wegelius;Jouni Uitto
从多形核白细胞中分离纯化了部分胶原酶，建立了一种测定胶原酶活性的新方法。该试验采用可溶性形式的天然放射性胶原作为底物。酶孵育在25°C下进行，该温度低于裂解产物TCA和TCB的熔化温度，这些肽通过聚丙烯酰胺凝胶电泳在十二烷基硫酸钠中定量回收。采用该方法，以I型胶原为底物，测定了人白细胞胶原酶的表观km值为1.04 × 10−6m。
Human collagenase was partially purified from polymorphonuclear leukocytes, and a new method for assay of the collagenase activity was developed. The assay employs native radioactive collagen in soluble form as a substrate. The enzyme incubations are performed at 25°C which is below the melting temperatures of the cleavage products TCA and TCB, and these peptides are quantitatively recovered by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Employing this method, an apparent Kmvalue of 1.04 × 10−6m for human leukocyte collagenase using type I collagen as a substrate was measured.