SOME BIOCHEMICAL AND PHYSICAL PROPERTIES OF THE HUMAN PERMEABILITY GLOBULINS,
Abstract
The permeability activity of globulin A is inhibited by C prime 1 esterase inhibitor, soy bean trypsin inhibitor, and di-isopropylfluorophosphate. TAMe portects against this DFP inhibition, and preparations of A contain SBTI inhibitable TAMe esterase. Preparations of A are also SBTI inhibitable kininogenases which liberate a smooth muscle contracting factor from both heated (63C, 1 hr.) and unheated plasma. A is estimated to have a sedimentation coefficient of approximately 11 S. It is concluded that globulin A is serum kallikrein. The permeability activity of globulin B is inhibited by C prime 1 esterase inhibitor, SBTI and DFP. TAMe protects against this DFP inhibition, and preparations of B contain SBTI inhibitable TAMe esterase. Preparations of globulin B are ineffective as kinin releasers when heated plasma (63C, 1 hr.) is used as the substrate. B is estimated to have a sedimentation coefficient of approximately 6 S. It is concluded that B is PF/dil. The inhibition of both permeability globulins by C prime 1 esterase inhibitor indicates that this inhibitor may be the permeability globulin inhibitor lacking in the disease, hereditary angioneurotic oedema. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 02, 1964
- Accession Number
- AD0612548
Entities
People
- L. J. Kagen
Organizations
- Walter Reed Army Institute of Research