Abstract
Insolubilized, radioodinated proteins are used as substrates for the assay of proteolytic activity. Trypsin hydrolysis of Sepharose-bound 125I-labeled casein, hemoglobin, immunoglobulin G, and bovine serum albumin (specific activities of 1–10 μCi/μg) is described to illustrate the sensitivity and applicability of this procedure. Over the course of a 5-min assay period, the activity of 0.1–5 μg of trypsin/ml is quantitated. Since 50 μl is used as the assay sample, this procedure is capable of detecting the equivalent of 5 ng of trypsin.
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