作者: Hiromu Nishihara , Satsuki Ishikawa , Kiyoko Shinkai , Hitoshi Akedo
DOI: 10.1016/0005-2744(73)90172-1
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摘要: Abstract 1. A conversion factor, which can convert the small form ( E S ; 47 000 mol. wt) of human adenosine deaminase (EC 3.5.4.4) to large L 230 wt), was purified about 600-fold from normal lung by (NH4)2SO4 fractionation, Sephadex and DEAE-cellulose chromatography, preparative acrylamide electrophoresis. 2. The preparation, heat labile free activity, exhibited upon disc electrophoresis a single protein band associated with converting activity also showed maximum absorption at 280 nm. Its molecular weight found be 139 when judged gel filtration G-200. 3. factor did not require sulfhydryl compounds nor bivalent metal ions for exerting its activity. 4. Results quantitative analysis rate formation known amounts , immunochemical characterizations two forms enzyme in relation using antiserum against polyacrylamide presence sodium dodecyl sulfate strongly suggest that is complex factor. 5. No detectable demonstrated an extract cancer tissue.