Isolation and Partial Characterization of a Low Molecular Weight Acid Stable Protease Inhibitor from Human Bronchial Secretion
- 1 January 1977
- journal article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 358 (1), 583-590
- https://doi.org/10.1515/bchm2.1977.358.1.583
Abstract
An acid stable protease inhibitor was isolated from human bronchial secretion. Two important stages of the purification procedure were affinity chromatography on trypsin bound to Affi-Gel 10 and ion-exchange chromatography on SP-Sephadex C-50. The isolated inhibitor appeared as a single band on analytical disc electrophoresis and eluted as a homogeneous protein peak on gel filtration on Sephadex G-75 corresponding to a molecular weight of about 10500. Amino acid analyses showed no tryptophan or histidine and as N-terminal amino acid tyrosine. No glucosamine or galactosamine was detected. The results of the analyses suggest that the purified inhibitor is identical to the low molecular weight trypsin-chymotrypsin inhibitor of human seminal plasma (HUSI-I).Keywords
This publication has 4 references indexed in Scilit:
- Identification et caracterisation des constituants proteiques de la secretion bronchique humaineClinica Chimica Acta; International Journal of Clinical Chemistry, 1976
- Inhibition of Elastase from Granulocytes by the Low Molecular Weight Bronchial Protease InhibitorScandinavian Journal of Clinical and Laboratory Investigation, 1976
- Ion-exchange chromatography of physiological sulphur amino acids on a highly crosslinked resinJournal of Chromatography A, 1972
- On the Determination of Cystine as Cysteic AcidJournal of Biological Chemistry, 1963