Isolation of bovine seminal ribonuclease by affinity chromatography |
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Authors: | W K Krietsch F C Simm B Hertenberger G W Kuntz E Wachter |
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Affiliation: | Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie der Universität München, Goethestrasse 33, 8000 Munich 2, West Germany |
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Abstract: | Pyrimidine base-specific RNase was isolated from bull semen by ammonium sulfate precipitation followed by affinity chromatography with ATP-ribosyl-adipoyldihydrazo-Sepharose. The enzyme is also bound to the AMP- or CMP-Sepharose gel. The binding capacity is 7 mg RNase/ml ATP-Sepharose. Using this procedure, a homogeneous protein with 74% yield could be isolated. The enzyme is a dimer with a molecular weight of 26,000. |
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