Reports

Ribonuclease Activity in Commercial Crystalline Trypsin and a Method for Removal

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Science  22 Nov 1968:
Vol. 162, Issue 3856, pp. 912-913
DOI: 10.1126/science.162.3856.912

Abstract

Several preparations of crystalline trypsin hydrolyze RNA because of contaminating ribonuclease activity. Filtration of these materials through Sephadex G-50 yields a trypsin devoid of ribonuclease activity and having a proteolytic specific activity about 70 percent of the starting material.

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