Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, V[1–4]. Attachments of Carbohydrates in the Human Urinary Trypsin Inhibitor Isolated by Affinity Chromatography
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (2) , 1357-1362
- https://doi.org/10.1515/bchm2.1981.362.2.1357
Abstract
The inhibitory active part of the inter-.alpha.-trypsin inhibitor with a known amino acid sequence is present as an acid-resistant inhibitor in human serum, in urine, in bronchial and in nasal mucus. The inhibitor molecule has a 50% carbohydrate content. Carbohydrate side chains are attached in 2 positions. One chain is linked to the polypeptide O-glycosidically via the serine residue in position 10 in the N-terminal extension peptide. The 2nd side chain is attached N-glycosidically via the asparagine residue in position 24, located in the inactive inhibitory Kunitz-type domain of the inhibitor. The compositions of the carbohydrate side chains were determined.This publication has 7 references indexed in Scilit:
- Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, IV. The Amino Acid Sequence of the Human Urinary Trypsin Inhibitor Isolated by Affinity ChromatographyHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1981
- Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, I. Determination of the Amino Acid Sequence of the Antitryptic Domain by Solid-Phase Edman DegradationHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, III. Sequence of the two Kunitz-Type Domains inside the Native Inter-α-Trypsin Inhibitor, Its Biological Aspects and also of Its Cleavage ProductsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, II. Characterization of a Second Inhibitory Inactive Domain by Amino Acid Sequence DeterminationHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Zur Charakterisierung der säurestabilen Proteaseninhibitoren aus HumanplasmaHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1973
- Purification and Properties of an Extracellular Protease of Staphylococcus aureusJournal of Biological Chemistry, 1972
- Über Hämoglobine, VI. Ein Verfahren zur präparativen Gewinnung natürlicher Peptide. Die Isolierung der tryptischen Spaltprodukte von Humanhämoglobin A über Dowex 1X2 unter Verwendung ninhydrinnegativer flüchtiger PufferHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1961