By W.S. Hoar, D.J. Randall and J.R. Brett (Eds.)
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Fine control of amino acid catabolism (via K,,,) has been convincingly illustrated in omnivorous mammals (Krebs, 1972). The tissue concentrations of most amino acids are normally less than 1 mM and K ,values of enzymes which degrade amino acids are millimolar or more. , postabsorptive or by increasing protein intake) will lead to a rapid increase in amino acid breakdown. Tissue levels of amino acids in fish may vary with species but recent analyses on channel catfish (Wilson and Poe, 1974) show that in liver, gills, and kidney they are greater than 1 mM.
The fact that even in starving fish the oxidation of substrates other than glucose takes precedence over the mobilization and hydrolysis of glycogen and oxidation of the resulting glucose suggests that the capacity of fish to oxidize glucose aerobically is somewhat limited. It also indicates that the demands of any tissues (presumably brain and nervous tissue) which catabolize glucose as a primary fuel are met by gluconeogenesis rather than b y glycogenolysis, blood glucose levels being maintained by the former process.
66 From Knox and Cowey (unpublished data). Results are given as the ratio of radioactivity incorporated by turbot fed a low-protein diet (6 g crude protein/100 g) to that of turbot fed a high-protein diet (50 g crude protein/100 9). ally similar in the carnivorous, poikilothermous fish and in the omnivorous, warm-blooded mammal. Appreciable quantities of the essential amino acids, leucine and phenylalanine, were also oxidized irrespective of the dietary protein level. This contrasts with the reduction in phenylalanine and leucine oxidation in the rat when dietary protein intake was reduced.
Bioenergetics and Growth by W.S. Hoar, D.J. Randall and J.R. Brett (Eds.)