Application of novel monoclonal antibodies in the purification, quantification, and immunohistological localization of the proteinase inhibitor α2-macroglobulin
Author:
Publisher
Elsevier BV
Subject
Applied Microbiology and Biotechnology,Biochemistry,Biotechnology,Bioengineering
Reference24 articles.
1. Demonstration of an α2 macroglobulin receptor in human fibroblasts, absent in tumor derived cell lines;Van Leuven;J. Biol. Chem.,1979
2. Human plasma proteinase inhibitors;Travis;Annu. Rev. Biochem.,1983
3. The interaction of α2 macroglobulin with proteinases;Barrett;Biochem. J.,1973
4. The electrophoretically “slow” and “fast” forms of α2 macroglobulin;Barrett;Biochem. J.,1979
5. Primary structure of α2 macroglobulin;Sottrup-Jensen;J. Biol. Chem.,1984
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1. Cell Surface-Bound Urokinase-Type Plasminogen Activator Facilitates Infiltration of Freshly Isolated Granulocytes into a Fibrin Matrix;Immunobiology;1995-11
2. Urokinase-type plasminogen activator enhances invasion of human T cells (Jurkat) into a fibrin matrix;Journal of Leukocyte Biology;1994-08
3. The autoimmune blistering skin disease bullous pemphigoid. The presence of plasmin/alpha 2-antiplasmin complexes in skin blister fluid indicates plasmin generation in lesional skin.;Journal of Clinical Investigation;1993-08-01
4. Immunohistochemical characterization of the plasminogen activator system in psoriatic epidermis;British Journal of Dermatology;1993-06
5. Plasminogen activation in lesional skin of Pemphigus vulgaris type Neumann;Archives of Dermatological Research;1993-01
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