Studies on lysyl oxidase of bovine ligamentum nuchae and bovine aorta.
Studies on lysyl oxidase of bovine ligamentum nuchae and bovine aorta.
复制标题
牛项韧带和主动脉赖氨酰氧化酶的研究。
DOI：
10.1007/978-1-4684-9093-0_44
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发表时间：
1977
影响因子：
--
通讯作者：
H. Kagan
中科院分区：
文献类型：
--
作者：
R. Jordan;P. Milbury;K. Sullivan;P. Trackman;H. Kagan
赖氨酰氧化酶已从牛主动脉和牛项韧带中纯化至接近同质，以及斯塔森和他的同事在DEAE纤维素上层析时，主动脉酶产生至少三个峰，韧带酶分解成至少四个峰。在十二烷基硫酸钠中，两种酶的每个峰的分子量约为30，000道尔顿。从尿素透析到磷酸盐缓冲盐水中后，主动脉酶聚集成分子量约为60，000至1，000，000道尔顿的物质。温度研究表明，赖氨酰氧化酶在高达80 ℃的温度下是稳定的，尽管测定的最佳温度是52 ℃。正在进行的研究表明，测定的温度依赖性可能反映了弹性蛋白底物的构象变化。
Lysyl oxidase had been purified to near homogeneity from bovine aorta and bovine ligamentum nuchae employing a modification of methods described by Harris et al., and Stassen and his colleagues. The aortic enzyme gives rise to at least three peaks and the ligament enzyme resolves into at least four peaks upon chromatography on DEAE cellulose. The molecular weight of each peak of both enzymes is approximately 30,000 daltons in sodium dodecyl sulfate. The aortic enzyme aggregates to species with molecular weights varying from approximately 60,000 to 1,000,000 daltons upon dialysis out of urea into phosphate-buffered saline. Temperature studies reveal that lysyl oxidase is stable to temperatures as high as 80 degrees C, although the assay optimum is 52 degrees C. Studies in progress suggest the temperature dependency of assay may reflect conformational changes in the elastin substrate.