Uricase from fish liver: Isolation and some properties

J. E. Kinsella; B. German; J. Shetty

doi:10.1016/0305-0491(85)90498-5

Uricase from fish liver: Isolation and some properties

J. E. Kinsella, B. German, J. Shetty

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Abstract

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 K_m and V_max values of 80 μM and > 1000 was obtained for the trout liver enzyme.

Original language	English (US)
Pages (from-to)	621-624
Number of pages	4
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	82
Issue number	4
DOIs	https://doi.org/10.1016/0305-0491(85)90498-5
State	Published - 1985
Externally published	Yes

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Medicine(all)

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Kinsella, J. E., German, B., & Shetty, J. (1985). Uricase from fish liver: Isolation and some properties. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 82(4), 621-624. https://doi.org/10.1016/0305-0491(85)90498-5

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author = "Kinsella, {J. E.} and B. German and J. Shetty",

year = "1985",

doi = "10.1016/0305-0491(85)90498-5",

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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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10.1016/0305-0491(85)90498-5