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Clinical Chemistry, Vol 20, 328-331, Copyright © 1974 by the American Association for Clinical Chemistry
1 Veterans Administration Hospital, and the Department of
Medicine, Emory University School of Medicine, Decatur, Ga.
30033.
Serum protease inhibitor activity was assessed from
the ability of the serum to inhibit casein hydrolysis by
-chymotrypsin (EC 3.4.4.5). Unmodified AutoAnalyzer equipment was used in conjunction with a fluorimetric method for dialyzable tyrosyl peptides.
Serum, diluted with tris(hydroxymethyl) aminomethane buffer, was added to a chymotrypsin solution to inhibit its activity. For 72 sera, the automated
method was compared with a manual determination
of trypsin inhibitor capacity. Results by the two
methods correlate well, supporting previous evidence that trypsin and chymotrypsin-inhibitor capacities of serum are related. The present automated method has several advantages that make it useful for clinical studies.
Submitted on July 30, 1973
Accepted on December 5, 1973
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