| Popis: |
β-Trypsin has been successfully modified by triethyloxonium fluoroborate and purified by means of affinity chromatography. Diethylated β-trypsin posseses relatively little activity towards arginine substrates which contain no other amino acids. In addition, there is considerable reduction in activity for the active site titrant, p -nitrophenyl- p '-guanidinobenzoate. However, there is no significant loss of the active site serine. The preparation of diethylated-β-trypsin demonstrates the feasibility for practically altering enzyme specificity, and increasing enzyme usefulness through such alteration. |
