scholarly journals "Life in a Germ-Free World": Isolating Life from the Laboratory Animal to the Bubble Boy

2012 ◽  
Vol 86 (2) ◽  
pp. 237-275 ◽  
Author(s):  
Robert G. W. Kirk
Keyword(s):  
Laboratory Animal ◽  
Free World ◽  
Germ Free

scholarly journals Sterilization of laboratory animal diets using gamma radiation

1969 ◽  
Vol 3 (2) ◽  
pp. 221-254 ◽  
Author(s):  
F. J. Ley ◽  
J. Bleby ◽  
Marie E. Coates ◽  
J. S. Paterson
Keyword(s):  
Radiation Dose ◽  
Adverse Effects ◽  
Gamma Radiation ◽  
General Health ◽  
Laboratory Animal ◽  
Suitable Method ◽  
Germ Free ◽  
And Storage

Sterilization by gamma radiation has proved to be a suitable method for the treatment of a variety of laboratory animal diets intended for specified-pathogen-free (SPF) and germ-free colonies. Due to the high penetrating power of this radiation the diets can be packed before treatment in a manner which prevents recontamination during transport and storage. The main bulk of diets is used for SPF animals and a radiation dose of 2.5 Mrad has proved effective for the control of contaminating organisms. No adverse effects on animals receiving the diets have been noted, observations having been made on growth, reproduction and general health. Irradiated diets formulated according to current laboratory animal practice appear to be nutritionally satisfactory.

Staphylococcal bacteremia in a "Germ-free" unit

1976 ◽  
Vol 136 (11) ◽  
pp. 1238-1240 ◽  
Author(s):  
M. E. Plaut
Keyword(s):  
Germ Free

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

1979 ◽  
Vol 42 (02) ◽  
pp. 726-733 ◽  
Author(s):  
Utako Okamoto ◽  
Jun-ichiro Yamamoto ◽  
Yoko Nagamatsu ◽  
Noboru Horie
Keyword(s):  
Serine Protease ◽  
Plasminogen Activator ◽  
Fibrinolytic Activity ◽  
Iodoacetic Acid ◽  
Thrombin Inhibitor ◽  
Rat Tissues ◽  
Germ Free ◽  
Neutral Ph ◽  
Tissue Extracts

SummaryProtease-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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