TY - JOUR
T1 - Uricase from fish liver
T2 - Isolation and some properties
AU - Kinsella, J. E.
AU - German, B.
AU - Shetty, J.
PY - 1985
Y1 - 1985
N2 - 1. 1. The uricase (urate: oxygen oxidoreducase EC.1.7.3.3) activities in livers from rainbow trout, mackerel, lake trout, catfish, shark and tilapia were 1000, 1180, 920, 630, 490 and 420 units (in moles uric acid oxidized mg-1 protein min-1) per gram liver, respectively. 2. 2. The enzyme from lake trout was purified twenty fold by ammonium sulfate precipitation, protamine sulfate treatment and Sephacryl S-200 column chromatography. 3. 3. SDS-polyacrylamide gel-electrophoresis indicated an oligomeric enzyme containing subunits of 32,500 daltons. 4. 4. The pH optimum was 8.8 but the enzyme had a relatively broad pH activity profile between pH 7.0-9.5. 5. 5. Apparent Km and Vmax values of 80 μM and > 1000 was obtained for the trout liver enzyme.
AB - 1. 1. The uricase (urate: oxygen oxidoreducase EC.1.7.3.3) activities in livers from rainbow trout, mackerel, lake trout, catfish, shark and tilapia were 1000, 1180, 920, 630, 490 and 420 units (in moles uric acid oxidized mg-1 protein min-1) per gram liver, respectively. 2. 2. The enzyme from lake trout was purified twenty fold by ammonium sulfate precipitation, protamine sulfate treatment and Sephacryl S-200 column chromatography. 3. 3. SDS-polyacrylamide gel-electrophoresis indicated an oligomeric enzyme containing subunits of 32,500 daltons. 4. 4. The pH optimum was 8.8 but the enzyme had a relatively broad pH activity profile between pH 7.0-9.5. 5. 5. Apparent Km and Vmax values of 80 μM and > 1000 was obtained for the trout liver enzyme.
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U2 - 10.1016/0305-0491(85)90498-5
DO - 10.1016/0305-0491(85)90498-5
M3 - Article
C2 - 4092430
AN - SCOPUS:0022296817
VL - 82
SP - 621
EP - 624
JO - Comparative biochemistry and physiology. B, Comparative biochemistry
JF - Comparative biochemistry and physiology. B, Comparative biochemistry
SN - 1096-4959
IS - 4
ER -