Paracoagulation of fibrinogen in vitro and in vivo by protein T of Steptococcus pyogenes.
Protein T was isolated from type 12 Streptococcus pyogenes cell wall by digestion with CNBr-sepharose linked trypsin and purified by ion exchange chromatography on QAE Sephadex A-50. Homogenous and not contaminated with other streptococcal proteins, antigen T, possesses paracoagulating activities similar to the effect of protamine sulphate. Protein T, applied intravenously to mice, accumulated mainly in kidneys and resulted in deposition of fibrinogen and its derivatives.
D000818:Animals; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D002473:Cell Wall / Q000032:analysis; D005340:Fibrinogen / Q000378:metabolism*; D007668:Kidney / Q000378:metabolism; D051379:Mice; D009928:Organ Specificity; D013297:Streptococcus pyogenes / Q000032:analysis
D001426:Bacterial Proteins; D005340:Fibrinogen