Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 153 - 162, Februar 1976 The Inter-a-Trypsin Inhibitor as Precursor of the Acid-Stable Proteinase Inhibitors in Human Serum and Urine Karl HOCHSTRASSER, Günther BRETZEL, Herbert FEUTH, Wolfgang HILLA and Kathrin LEMPART Klinik für Hals-, Nasen- und Ohrenkranke der Universität München (Received 20 October 1975) Summary: A small amount of antitryptic activity is detectable in the supernatant of deproteinized human serum. Preincubation of serum with trypsin causes an increase in acid-stable antitryptic activity. This rise in activity depends on the inter-trypsin inhibitor concentration. The native inhibitor present in normal sera, and in higher concentrations in sera of patients with nephropathies, and the trypsin-liberated inhibitor show immunological cross reaction with antibodies to the serum inter-a-trypsin inhibitor. The two inhibitors differ in molecular weight and electrophoretic mobility. The physiological inhibitor (1-34), with a molecular weight of 34000 and a high carbohydrate content, can be transformed by trypsin into an inhibitor (1-17) with a molecular weight of 17 000. This inhibitor is identical with the inhibitors liberated by trypsin from serum or from purified inter-a-trypsin inhibitor. The acid-stable inhibitor from urine is identical with the physiological serum inhibitor. Analogously, this inhibitor is transformed by trypsin
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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