-Essential amino acids (EAA) are responsible for skeletal muscle anabolic effects after nutrient intake. The pattern of appearance of EAA in blood, e.g., after intake of "slow" or "fast" protein sources or in response to grazing vs. bolus feeding patterns, may impact anabolism. However, the influence of this on muscle anabolism is poorly understood, particularly in older individuals. We determined the effects of divergent feeding profiles of EAA on blood flow, anabolic signaling, and muscle protein synthesis (MPS) in older men. Sixteen men (ϳ70 yr) consumed EAA either as a single dose (bolus, 15 g; n ϭ 8) or as small repeated fractions (pulse, 4 ϫ 3.75 g every 45 min; n ϭ 8) during 13 C6 phenylalanine infusion. Repeated blood samples and muscle biopsies permitted measurement of fasting and postprandial plasma EAA, insulin, anabolic signaling, and MPS. Muscle blood flow was assessed by contrast-enhanced ultrasound (Sonovue). Bolus achieved rapid insulinemia (12.7 iU/ml 25-min postfeed), essential aminoacidemia (ϳ3,000 M, 45-65 min postfeed), and mTORC1 activity; pulse achieved attenuated insulin responses, gradual low-amplitude aminoacidemia (ϳ1,800 M 80-195 min after feeding), and undetectable mTORC1 signaling. Despite this, equivalent anabolic responses were observed: fasting FSRs of 0.051 and 0.047%/h (bolus and pulse, respectively) increased to 0.084 and 0.073%/h, respectively. Moreover, pulse led to sustainment of MPS beyond 180 min, when bolus MPS had returned to basal rates. We detected no benefit of rapid aminoacidemia in this older population despite enhanced anabolic signaling and greater overall EAA exposure. Rather, apparent delayed onset of the "muscle-full" effect permitted identical MPS following low-amplitude-sustained EAA exposure. protein synthesis; nutrition; amino acids; skeletal muscle; anabolic signaling; muscle full state IN HEALTHY AND HABITUALLY ACTIVE ADULTS, muscle mass remains constant over early life to midlife, demonstrating effective proteostatic mechanisms balancing the synthesis and breakdown of muscle proteins. Beyond the sixth decade, however, breakdown of muscle proteins exceeds synthesis, and muscle mass is gradually lost. This results in muscle atrophy and frailty (36) referred to as sarcopenia, which is of great significance to an aging population,with decrements in muscle mass and strength being predictors of illness, loss of independence, and death (14,31,32,41,51).One facet that may contribute to sarcopenia is anabolic resistance, a compromised anabolic response to protein/essential amino acid (EAA) consumption with decreased postprandial muscle protein synthesis (MPS) (15, 27, 52). Moreover, a preferential loss of lean tissue over fat in older age (24) and a tendency to consume less high-quality protein (39, 46) may exacerbate such anabolic resistance. The total anabolic value of one meal is limited, with a modest intake of high-quality protein maximally stimulating MPS and no additional benefit from excessive protein ingestion (48), although some have suggested that inc...