Elsevier

Methods in Enzymology

Volume 45, 1976, Pages 760-772
Methods in Enzymology

[66]The inter-α-trypsin inhibitor

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Publisher Summary

An a-glycoprotein, called protein π (the Greek letter π standing for Paris), was isolated from human plasma by Steinbuch and Loeb. Heimburger and Schwick showed that a protein migrating in the inter-a-region (between al- and a2-globulivns), had an inhibitory activity against trypsin. Heide et al. purified the active component and called it inter-a-trypsin inhibtor (IaI). This protein proved later to be identical with protein π. This chapter elaborates the various assay methods: assay in whole serum (Semiquantitative Methods, such as Fibrin-Agar Electrophoresis and Quantitative Methods). Techniques for assay of purified IαI as well as isolation techniques (Heimburger et al. and Steinbuch et al.) have been covered. Properties such as stability and other properties, physical and chemical properties, kinetic properties, distribution, relation to other inhibitors have been discussed in this chapter

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