Thromb Haemost 1979; 42(02): 726-733
DOI: 10.1055/s-0038-1666910
Original Article
Schattauer GmbH Stuttgart

Fibrinolytic Activity of Lung and Spleen Extracts Observed in Conventional but not in Germ-Free Rats

Utako Okamoto
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University Ikawadani, Tarumi-ku, Kobe 673, Japan
,
Jun-ichiro Yamamoto
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University Ikawadani, Tarumi-ku, Kobe 673, Japan
,
Yoko Nagamatsu
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University Ikawadani, Tarumi-ku, Kobe 673, Japan
,
Noboru Horie
The Department of Physiology, Faculty of Nutrition, Kobe-Gakuin University Ikawadani, Tarumi-ku, Kobe 673, Japan
› Author Affiliations
Further Information

Publication History

Received 14 August 1978

Accepted 29 September 1978

Publication Date:
23 August 2018 (online)

Summary

Protease-like activity which split plasminogen-free fibrin was demonstrated in 2 M KSCN extracts of the lung and spleen of conventional rats. The activity was virtually undetectable in tissue extracts from germ-free rats. The extracts from the conventional rat tissues split fibrin and fibrinogen remarkably at neutral pH, but not casein, when examined using fibrin, fibrinogen-agar and casein-agar plates. The fibrinolytic activity was inhibited by STI and DFP, indicating a serine protease nature. The activity was not inhibited by TLCK, t-AMCHA or dansyl-L-arginine-methylpiperidine amide (a selective synthetic thrombin inhibitor, OM189). It was neither activated nor inhibited by cysteine, KCN or iodoacetic acid. The results obtained indicate that the protease-like activity of the lung and spleen extracted with 2 M KSCN from conventional rats has properties which differ from those of trypsin, plasmin, plasminogen-activator, thrombin, and cathepsin A, B and C.

 
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