Partition of Trypsin and Kazal Inhibitor in Reaction Mixtures with Human Serum

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Abstract
The partition of trypsin and pancreatic secretory trypsin inhibitor (PSTI) in reaction mixtures with human serum was studied by electroimmunoassay and gel filtration on Sephadex G-200. The same pattern of trypsin complexes with .alpha.2-macroglobulin and .alpha.1-antitrypsin was observed in the presence or absence of PSTI. When sufficient trypsin was added to saturate the .alpha.2-macroglobulin, more complex with .alpha.1-antitrypsin was formed. A small amount of PSTI-trypsin complex was formed only when large amounts of trypsin and PSTI were present. The majority of PSTI was found in the fractions containing .alpha.2-macroglobulin, indicating the formation of a PSTI-trypsin-.alpha.2-macroglobulin complex. The remaining PSTI was eluted as free inhibitor. Increasing the added PSTI increased the fraction eluted as free inhibitor. .alpha.1-Antitrypsin and .alpha.2-macroglobulin appear to be much stronger than PSTI in their competition for trypsin in reaction mixtures of human serum, trypsin and PSTI.

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