Identification of a plasma gelatinase in preparations of fibronectin.
作者： S Johansson , B Smedsrød
DOI: 10.1016/S0021-9258(17)38507-1
关键词:
摘要: Preparations of fibronectin purified from human plasma according to conventional methods was found contain a latent gelatinolytic activity. The protease activated by exposure trypsin or electrophoresis in sodium dodecyl sulfate. Zymography the enzyme under nonreducing conditions gave an estimated Mr 72,000. Reducing agents destroyed activity enzyme. gelatinase co-purified with chromatography on Sepharoses conjugated gelatin, arginine, and heparin but could be separated gel filtration physiological buffer. This normal constituent probably not derived blood cells since 72-kDa detected lysates these cells.
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