Abstract
In 1961 Steinbuch and Loeb (1961) described a new plasma protein named protein π. A few years later, Heide et al. (1965) purified a new plasma proteinase inhibitor, inter-a-trypsin inhibitor (ITI). These two proteins proved to be identical. ITI is a single-chain, very labile, Zn-containing glycoprotein (Steinbuch, 1976). It is a reversible inhibitor of serine proteinases which is much more potent on bovine trypsin (Ki = 2.1 x 10-11 M) than on bovine chymotrypsin (Ki = 1.08 x 10-09 M) (Aubry and Bieth, 1976). ITI inhibits human pancreatic trypsin and chymotrypsin with much less efficiency (Aubry and Bieth, 1976) and is inactive against porcine pancreatic elastase (Meyer et al., 1975). The physiological function of ITI is not well understood.
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© 1988 Plenum Press, New York
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Gast, A., Bieth, J.G. (1988). Inhibition of Human Neutrophil Elastase by Acid-Soluble Inter-α-Trypsin Inhibitor. In: Hörl, W.H., Heidland, A. (eds) Proteases II. Advances in Experimental Medicine and Biology, vol 240. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1057-0_8
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DOI: https://doi.org/10.1007/978-1-4613-1057-0_8
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