The Biology and Biochemistry of Antichymotrypsin and its Potential Role as a Therapeutic Agent
- 1 January 1992
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 373 (2) , 497-502
- https://doi.org/10.1515/bchm3.1992.373.2.497
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Crystal structure of cleaved human α1-antichymotrypsin at 2.7 å resolution and its comparison with other serpinsJournal of Molecular Biology, 1991
- Acute phase protein stimulation by alpha 1-antichymotrypsin-cathepsin G complexes. Evidence for the involvement of interleukin-6.Journal of Biological Chemistry, 1990
- Mast cell chymase potentiates histamine-induced wheal formation in the skin of ragweed-allergic dogs.Journal of Clinical Investigation, 1990
- Serum Protein Changes after Abdominal SurgeryAnnals of Clinical Biochemistry: International Journal of Laboratory Medicine, 1989
- In vivo catabolism of α1-antichymotrypsin is mediated by the Serpin receptor which binds α1-proteinase inhibitor, antithrombin III and heparin cofactor IIBiochimica et Biophysica Acta (BBA) - General Subjects, 1988
- Synthesis and release of platelet-activating factor is inhibited by plasma alpha 1-proteinase inhibitor or alpha 1-antichymotrypsin and is stimulated by proteinases.The Journal of Experimental Medicine, 1988
- Purification and identification of two serine class proteinases from dog mast cells biochemically and immunologically similar to human proteinases tryptase and chymaseArchives of Biochemistry and Biophysics, 1988
- Human serum α1‐antichymotrypsin is an inhibitor of pancreatic elastasesEuropean Journal of Biochemistry, 1985
- The synthesis of a proteinase inhibitor, α‐1‐antichymotrypsin, by human breast epithelial cellsJournal of Supramolecular Structure and Cellular Biochemistry, 1981
- Presence of α1-Antichymotrypsin and α1-Antitrypsin in Haematopoietic and Lymphoid Tissue Cells as Revealed by the Immunoperoxidase MethodPathology - Research and Practice, 1980