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Original Article

Purification of Canine Pancreatic Secretory Trypsin Inhibitor and Interaction in Vitro with Complexes of Trypsin- α -Macroglobulin

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Pages 815-820 | Received 16 Feb 1976, Accepted 11 Oct 1976, Published online: 08 Jul 2009
 

Abstract

Highly purified pancreatic secretory trypsin inhibitor (PSTI) from the dog was found to exist in three different chromatographic forms with equal capacities for the inhibition of trypsin. The molecular weight of the inhibitor, calculated from sodium dodecyl sulfate electrophoresis was approximately 7,000. It was capable of blocking proteolytic activity of the trypsin-α-macroglobulin complex even though inhibition was never complete.

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