1. The purine nucleotide cycle has been proposed (Lowenstein, 1972) as an alternative scheme for amino acid deamination in tissues, such as skeletal muscle, having low concentrations of glutamate dehydrogenase (EC 1.4.1.2).2. Activities of AMP deaminase (EC 3.5.4.6), one of the enzymes of the cycle, have been measured in soleus, plantaris and extensor digitorum longus muscles of rats maintained for 18 d on diets providing 0, 0·035 or 0·10 net dietary protein energy (energy supplied by utilizable protein: total metabolizable energy, NDp:E), and in rats given the 0·10 NDp:E diet for 3 d after the 0 or 0·035 NDp:E regimens.3. Concentration of AMP deaminase in the different muscles from the control (0·10 NDp:E diet) rats appeared to bear an inverse relationship to the proportion of mitochondria-rich fibres (i.e. rich in glutamate dehydrogenase) in each muscle.4. Dietary protein deprivation (0 or 0·035 NDp:E) led to adaptive reductions in AMP-deaminase activity in the soleus and plantaris muscles, but in the extensor muscle the 0·035 NDp:E diet produced no change, while the 0 NDp:E diet caused an increase in activity.5. Refeeding the 0·10 NDp:E diet to the protein-deprived rats caused reductions of AMP-deaminase activity to lower levels in all three muscles, except in the instance of soleus in rats refed after the 0·035 NPp:E diet.6. In view of the different responses shown by the three muscles to the dietary treatments, the importance of specifying the particular muscles used in future nutritional studies is emphasized.7. The adaptive changes in AMP deaminase are discussed in terms of operation of the purine nucleotide cycle for amino acid deamination responding to the changes in amino acid catabolism known to be caused in muscle by these protein-deficient diets.
Effects of dietary protein, energy and β-mannanase on laying performance, egg quality, and ileal amino acid digestibility in laying hens.
