Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1914 Jul 1;20(1):37–51. doi: 10.1084/jem.20.1.37

THE MECHANISM OF ANAPHYLATOXIN FORMATION

STUDIES ON FERMENT ACTION. XV.

James W Jobling 1, William Petersen 1
PMCID: PMC2125178  PMID: 19867801

Abstract

1. The unsaturated lipoids (serum antitrypsin) can be adsorbed from guinea pig serum, rabbit serum, and horse serum by kaolin, starch, agar, and bacteria. 2. Diphtheria toxin and cobra venom also reduce the serum antitrypsin, possibly because of their affinity for lipoids. 3. Anaphylatoxins represent sera rendered toxic by partial removal of serum antitrypsin. 4. The matrix of the protein split products lies in the serum proteins so exposed. 5. The amount of removal of serum antitrypsin depends on definite quantitative relations; very large amounts and very small amounts of adsorbing substances are least effective (kaolin, starch, and bacteria). 6. Bacteria previously treated with serum or with oils do not adsorb serum antitrypsin. 7. Bacteria treated with serum become more resistant to the action of trypsin.

Full Text

The Full Text of this article is available as a PDF (659.8 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Jobling J. W., Petersen W. THE NATURE OF SERUM ANTITRYPSIN : STUDIES ON FERMENT ACTION. XIII. J Exp Med. 1914 May 1;19(5):459–479. doi: 10.1084/jem.19.5.459. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES