Degradation of bovine complement C3 by trichomonad extracellular proteinase

Author:

Kania S.A.,Reed S.L.,Thomford J.W.,BonDurant R.H.,Hirata K.,Corbeil R.R.,North M.J.,Corbeil L.B.

Publisher

Elsevier BV

Subject

General Veterinary,Immunology

Reference53 articles.

1. Human C’3: evidence for the liver as the primary site of synthesis;Alper;Science,1969

2. Differential cytokine regulation of complement C3, C4, and factor B synthesis in human epithelial cell line Caco-2;Andoh;J. Immun.,1993

3. Antibody enhances killing of Tritrichomonas foetus by the alternative bovine complement pathway;Aydintug;Infect. Immunol.,1990

4. Bovine polymorphonuclear leukocyte killing of Tritrichomonas foetus;Aydintug;Infect. Immunol.,1993

5. Cleavage of purified bovine complement component C3 in larval Hypoderma lineatum (Diptera: Oestridae) hypodermins;Baron;J. Med. Entomol.,1990

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