Biomedical subjects
Publications and source records attributed to N E Garrison.
1. Isolation conditions for rainbow trout (Salmo gairdneri) liver ribosomes were optimized. 2. Optimal initial buffer (Buffer I) concentrations were 250 mM sucrose, 50 mM Tris (pH 7.6, 25 degrees C), 75 mM KCl, and 5 mM MgSO4.7H2O. 3. Optimal concentrations for post-105 supernatant buffer (Buffer III) were 25 mM Tris (pH 7.6, 25 degrees C), 75 mM KCl, and 8 mM MgSO4.7H2O.
The ability of rat liver ribosomes to support in vitro protein synthesis was not adversely affected, and generally tended to increase as the centrifugal force at which they were isolated increased. Polysomal material tended to decrease while 40S and 60S ribosomal subunits apparently increased at progressively higher centrifugal forces. Ribosomal "purity", revealed by u.v. spectrophotometric analysis, deteriorated as centrifugal force increased. Contamination by material that absorbed at 230 nm was particularly evident.
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1. Liver microsomal quantity decreased in young rats 2 days after partial hepatectomy or sham operation, increased to preoperative values by 8 days, and remained unchanged 16 days following surgery. 2. In old rats, microsomal quantity remained unchanged following surgery, but increased in sham-operated controls. 3. Translational efficiency of microsomes from young, sham-operated animals was unaffected, but decreased 2 days after partial hepatectomy. 4. In old, sham-operated controls, efficiency decreased, but remained unchanged 2 days after partial hepatectomy. 5. Eight and 16 days after surgery, efficiency of microsomes from young and old animals appeared indistinguishable, and were similar to those of adults before surgery.
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The distribution of activity similar to that of one of the initiation factors (IF2) was determined as a function of developmental stage in Xenopus laeviseggs and embryos. In vivo exposure of mature oocytes to hormone increases the total amount of detectable factor activity and facilitates the binding of IF2-like factor to ribosomes. The quality of factor bound is not correlated with polysome content.
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