Abstract
Decrease in the protease activity of the culture fluid observed at later stages of the antigen-antibody reaction is believed to be due to the release of an inhibitor by the cells. The inhibitor was submitted to partial purification: it is heat-stable, non-precipitated by trichloracetic acid and non-dialyzable. It inhibits certain cellular and tissue proteases and papain but is inactive against trypsin. It is suggested that the balance between protease and anti-protease released may determine the intensity, extent, and duration of certain sensitization phenomena.
Full Text
The Full Text of this article is available as a PDF (320.1 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- FINKENSTAEDT J. T. Intracellular distribution of proteolytic enzymes in rat liver tissue. Proc Soc Exp Biol Med. 1957 Jun;95(2):302–304. doi: 10.3181/00379727-95-23201. [DOI] [PubMed] [Google Scholar]
- GREENBAUM L. M., FRUTON J. S. Purification and properties of beef spleen cathepsin B. J Biol Chem. 1957 May;226(1):173–180. [PubMed] [Google Scholar]
- GROB D. Proteolytic enzymes; further studies on protein, polypeptide, and other inhibitors of serum proteinase, leucoproteinase, trypsin, and papain. J Gen Physiol. 1949 Nov;33(2):103–124. doi: 10.1085/jgp.33.2.103. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HAYASHI H., TOKUDA A., UDAKA K. Biochemical study of cellular antigen-antibody reaction in tissue culture. I. Activation and release of a protease. J Exp Med. 1960 Aug 1;112:237–247. doi: 10.1084/jem.112.2.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
