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Complete suppression of protein synthesis during anoxia with no post-anoxia protein synthesis debt in the red-eared slider turtle Trachemys scripta elegans

Keiron P. P. Fraser1,*, Dominic F. Houlihan1, Peter L. Lutz2, Sandra Leone-Kabler2, Liscia Manuel2 and James G. Brechin1

1 Department of Zoology, University of Aberdeen, Tillydrone Avenue, Aberdeen AB24 3TZ, UK and
2 Department of Biological Sciences, Florida Atlantic University, Boca Raton, FL 33141, USA



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Fig. 1. Intracellular free-pool phenylalanine specific radioactivities in the intestine, heart, liver, brain, muscle and lung of anoxia-exposed (filled circles) and normoxia-exposed (open circles) turtles. N=6 except for the muscle 1 h of anoxia value, where N=3. Values are means ± S.E.M. (experiment 1).

 


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Fig. 2. Protein-incorporated phenylalanine specific radioactivities in the intestine (y=0.810x+0.27, r2=0.252, N=18), heart (y=0.277x–0.003, r2=0.330, N=18), liver (y=1.6x–0.76, r2=0.374, N=18), brain (y=0.709x–0.304, r2=0.363, N=18), muscle (y=0.164x+0.051, r2=0.382, N=15) and lung (y=0.163x+0.366, r2=0.233, N=18) of anoxia-exposed (filled circles) and normoxia-exposed (open circles) turtles. Regression equations refer to normoxic protein-incorporated phenylalanine specific radioactivities. All r2 values are significant (P<0.05), and the intercepts were not significantly different from zero in any tissue. N=6 except for the muscle 1 h of anoxia value, where N=3. Values are means ± S.E.M. (experiment 1).

 


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Fig. 3. Fractional rates of protein synthesis in the intestine, heart, liver, brain, muscle and lung of turtles exposed to 3 h of normoxia (N) and 0.5 h (0.5R), 1 (1R) or 3 h (3R) of recovery from anoxia. Values are means + S.E.M. (N=6). Values marked with an asterisk are significantly different from one another within a tissue (experiment 2).

 





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