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HUMAN INTER-ALPHA-TRYPSIN INHIBITOR - LIMITED PROTEOLYSIS BY TRYPSIN, PLASMIN, KALLIKREIN AND GRANULOCYTIC ELASTASE AND INHIBITORY PROPERTIES OF THE CLEAVAGE PRODUCTS
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INTER-ALPHA-TRYPSIN INHIBITOR AS PRECURSOR OF ACID-STABLE PROTEINASE-INHIBITORS IN HUMAN-SERUM AND URINE
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KUNITZ-TYPE PROTEINASE-INHIBITORS DERIVED BY LIMITED PROTEOLYSIS OF THE INTER-ALPHA-TRYPSIN INHIBITOR .1. DETERMINATION OF THE AMINO-ACID SEQUENCE OF THE ANTI-TRYPTIC DOMAIN BY SOLID-PHASE EDMAN DEGRADATION
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KUNITZ-TYPE PROTEINASE-INHIBITORS DERIVED BY LIMITED PROTEOLYSIS OF THE INTER-ALPHA-TRYPSIN INHIBITOR .5. ATTACHMENTS OF CARBOHYDRATES IN THE HUMAN URINARY TRYPSIN-INHIBITOR ISOLATED BY AFFINITY-CHROMATOGRAPHY
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KUNITZ-TYPE PROTEINASE-INHIBITORS DERIVED BY LIMITED PROTEOLYSIS OF THE INTER-ALPHA-TRYPSIN INHIBITOR .6. DETECTION OF A COMPLEX BETWEEN IMMUNOGLOBULIN-G AND THE INHIBITORY ACTIVE PART OF THE INTER-ALPHA-TRYPSIN INHIBITOR
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KUNITZ-TYPE PROTEINASE-INHIBITORS DERIVED BY LIMITED PROTEOLYSIS OF THE INTER-ALPHA-TRYPSIN INHIBITOR .3. SEQUENCE OF THE 2 KUNITZ-TYPE DOMAINS INSIDE THE NATIVE INTER-ALPHA-TRYPSIN INHIBITOR, ITS BIOLOGICAL ASPECTS AND ALSO OF ITS CLEAVAGE PRODUCTS
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KUNITZ-TYPE PROTEINASE-INHIBITORS DERIVED BY LIMITED PROTEOLYSIS OF THE INTER-ALPHA-TRYPSIN INHIBITOR .2. CHARACTERIZATION OF A 2ND INHIBITORY INACTIVE DOMAIN BY AMINO-ACID SEQUENCE DETERMINATION
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