THE BIOLOGICAL SIGNIFICANCE AND CHEMISTRY OF A PROTEASE INHIBITOR NEWLY ISOLATED FROM ANIMAL TISSUES
Abstract
Studies on the euglobulin fraction, prepared from the subsiding or healing site of cutaneous Arthus inflammation in rabbits, can suppress markedly the inflammation; and the suppressing effect of the protein fraction is largely due to a specific pro tease inhibitor present in the protein fraction are presented. This previously undescribed anti protease was extensively purified and obtained as fibrous crystalline-like substance; the purifi cation procedures essentially consisted of frac tionation with ammonium sulfate, chromatography with Sephadex G-50 and DEAE-cellulose, and con centration with Sephadex G-25. This antiprotease inactivated a particular SH-dependent protease of the cutaneous lesion of Arthus inflammation and papain, but had no effect on trypsin and chymo trypsin. This substance appeared to be a poly peptide, pisitive with biuret test, thermostable, non-diffusible, non-precipitable with 3% trichlo roacetic acid and insoluble in water but soluble in salt. The mechanism of increased vascular permeability in inflammation was studied because this phenomenon is one of the cardinal features in inflammation. A new permeability factor (PF) was isolated as the pseudoglobulin fraction from the lesion showing the delayed response; the substance was insusceptible to antihistamine, soy bean trypsin inhibitor, or di-iso-propyl phospho fluoridate, and had no smooth muscle-stimulating action or chemotactic action on leucocytes.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 31, 1963
- Accession Number
- AD0409315
Entities
People
- Hideo Hayashi
Organizations
- Kumamoto University