作者: Nathan N. Aronson , Eugene A. Davidson
DOI: 10.1016/S0021-9258(18)96291-5
关键词: Polyacrylamide gel electrophoresis 、 Hydroxylapatite 、 Sedimentation equilibrium 、 Chromatography 、 Hyaluronidase 、 Electrophoresis 、 Ammonium sulfate precipitation 、 Chemistry 、 Ultracentrifuge 、 Sephadex 、 Biochemistry
摘要: Hyaluronidase isolated from the lysosomes of rat liver (1) was purified 1300-fold by ammonium sulfate precipitation, chromatography on hydroxylapatite, and Sephadex G-100. The most fraction gave two peaks sedimentation in ultracentrifuge, faster being yellow possessing no enzymic activity. slower peak showed a single band acrylamide gel electrophoresis. molecular weight enzyme calculated to be 89,000 based equilibrium data.