It is now generally believed that elderly may have slightly higher dietary protein requirements than those of the young-middle-aged adults. We have previously conducted related studies by the indicator amino acid oxidation (IAAO) technique, but more research data are needed to revise the protein requirements of the elderly. The main objective was to reevaluate the dietary protein requirements of healthy Chinese adults (65–80 years) without sarcopenia by using the IAAO technique. Nine healthy adult men and seven healthy adult women participated in the study, with protein intakes ranging from 0·1 to 1·8 g/(kg·d). Diets that delivered energy at a 1·5 resting energy expenditure were isocaloric. The amounts of phenylalanine and tyrosine needed to remain constant for each protein dosage. By applying a nonlinear mixed-effects model analysis on the F13CO2 data, which revealed a breakpoint in F13CO2 in response to graded protein intakes, the mean protein requirement was calculated. The mean estimated average requirement (EAR) for healthy elderly Chinese adults without sarcopenia was determined to be 0·94 g/(kg·d). The protein recommended nutrient intake (RNI) determined using various derivation approaches ranged from 1·13 to 1·36 g/(kg·d). The EAR for Chinese adults without sarcopenia aged 65–80 years in this study is 6·8 % higher than the current recommended EAR (0·88 g/(kg·d)). The RNI derived using various derivation approaches are all greater than the current RNI (0·98 g/(kg·d)). This trial was registered with the Chinese clinical trial registry as ChiCTR2200061382.

Intravenous infusion of L-[3H] phenylalanine (Phe) was carried out for 8 h in dry, non-pregnant and lactating dairy goats. Nitrogen balance was positive in the dry group and negative in the lactating group. Whole-body Phe flux was 50% greater in lactating goats (P < 0.01). Fractional synthesis rates (Ks) of tissue proteins were estimated from plasma- (Ksp) and tissue- (Ksh) specific radioactivities of Phe. In lactating goats, Ksp for mammary gland, duodenum and diaphragm was increased (P < 0.05). Ksp also tended to increase in liver, kidney and rumen (P < 0.08) of lactating goats, but was not different in uterus, spleen, caecum or heart. Values of Ksh were higher than Ksp; however, these measures agreed qualitatively. When absolute rates of protein synthesis were calculated, an increased contribution of mammary and visceral organs was seen in lactating goats. Ks and absolute rates of protein synthesis of hind-limb skin were less in lactating goats (P < 0.05). A decreased proportion of skeletal muscle (P < 0.01) and decreased Ks resulted in lower absolute synthesis of hind-limb muscle protein in lactating animals (P < 0.05). Decreased rates of muscle and skin protein synthesis would appear to participate in alterations of protein metabolism, permitting lactation to occur at the expense of body reserves.